A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
TRANSPORT VESICLES formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of COP (coat protein complex) proteins, either COPI or COPII. COPI coated vesicles transport backwards from the cisternae of the GOLGI APPARATUS to the rough endoplasmic reticulum (ENDOPLASMIC RETICULUM, ROUGH), while COPII coated vesicles transport forward from the rough endoplasmic reticulum to the Golgi apparatus.
ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A flavoprotein and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 1.6.99.3.
A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
A bacteriophage genus of the family LEVIVIRIDAE, whose viruses contain the short version of the genome and have a separate gene for cell lysis.
Viruses whose hosts are bacterial cells.
The outer protein protective shell of a virus, which protects the viral nucleic acid.
Bacteriophages whose genetic material is RNA, which is single-stranded in all except the Pseudomonas phage phi 6 (BACTERIOPHAGE PHI 6). All RNA phages infect their host bacteria via the host's surface pili. Some frequently encountered RNA phages are: BF23, F2, R17, fr, PhiCb5, PhiCb12r, PhiCb8r, PhiCb23r, 7s, PP7, Q beta phage, MS2 phage, and BACTERIOPHAGE PHI 6.
Viruses whose host is Escherichia coli.
A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Proteins that form the CAPSID of VIRUSES.
The genetic complement of an organism, including all of its GENES, as represented in its DNA, or in some cases, its RNA.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The addition of descriptive information about the function or structure of a molecular sequence to its MOLECULAR SEQUENCE DATA record.
Databases devoted to knowledge about specific genes and gene products.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
The systematic study of the complete DNA sequences (GENOME) of organisms.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A DNA repair enzyme that catalyses the excision of ribose residues at apurinic and apyrimidinic DNA sites that can result from the action of DNA GLYCOSYLASES. The enzyme catalyzes a beta-elimination reaction in which the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. This enzyme was previously listed under EC 3.1.25.2.
An enzyme which catalyzes the endonucleolytic cleavage of phosphodiester bonds at purinic or apyrimidinic sites (AP-sites) to produce 5'-Phosphooligonucleotide end products. The enzyme prefers single-stranded DNA (ssDNA) and was formerly classified as EC 3.1.4.30.
Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.
A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.
OXIDOREDUCTASES which mediate vitamin K metabolism by converting inactive vitamin K 2,3-epoxide to active vitamin K.
A large protein complex which acts as a signaling adaptor protein that allows communication between the various regulatory and functional components of GENETIC TRANSCRIPTION including DNA POLYMERASE II; GENERAL TRANSCRIPTION FACTORS; and TRANSCRIPTION FACTORS that are bound to upstream ENHANCER ELEMENTS. The mediator complex was originally studied in YEAST where at least 21 subunits were identified. Many of the yeast subunits are homologs to proteins in higher organisms that are found associated with specific nuclear receptors such as THYROID HORMONE RECEPTORS and VITAMIN D RECEPTORS.
A conserved AMINO ACID SEQUENCE located in the intracellular domains of a family of transmembrane proteins involved in various IMMUNE RESPONSES. The CONSENSUS SEQUENCE of this motif is YXXL(or I)X(6-8)YXXL(or I) (where X denotes any amino acid). When phosphorylated ITAM motifs provide docking sites for PROTEIN TYROSINE KINASES of the Syk family thus forming signaling complexes which lead to activation of immune responses.
A form of long QT syndrome that is associated with congenital deafness. It is characterized by abnormal cardioelectrophysiology involving the VOLTAGE-GATED POTASSIUM CHANNEL. It results from mutation of KCNQ1 gene (Subtype 1 or JLN1) or the KCNE1 gene (Subtype 2 or JLN2).
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
Particles consisting of aggregates of molecules held loosely together by secondary bonds. The surface of micelles are usually comprised of amphiphatic compounds that are oriented in a way that minimizes the energy of interaction between the micelle and its environment. Liquids that contain large numbers of suspended micelles are referred to as EMULSIONS.
Disruption of the secondary structure of nucleic acids by heat, extreme pH or chemical treatment. Double strand DNA is "melted" by dissociation of the non-covalent hydrogen bonds and hydrophobic interactions. Denatured DNA appears to be a single-stranded flexible structure. The effects of denaturation on RNA are similar though less pronounced and largely reversible.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Heterogeneous group of autosomal recessive disorders comprising at least four recognized types, all having in common varying degrees of hypopigmentation of the skin, hair, and eyes. The two most common are the tyrosinase-positive and tyrosinase-negative types.
Melanin-containing organelles found in melanocytes and melanophores.
Syndrome characterized by the triad of oculocutaneous albinism (ALBINISM, OCULOCUTANEOUS); PLATELET STORAGE POOL DEFICIENCY; and lysosomal accumulation of ceroid lipofuscin.
Color of the iris.
Mammalian pigment cells that produce MELANINS, pigments found mainly in the EPIDERMIS, but also in the eyes and the hair, by a process called melanogenesis. Coloration can be altered by the number of melanocytes or the amount of pigment produced and stored in the organelles called MELANOSOMES. The large non-mammalian melanin-containing cells are called MELANOPHORES.
General term for a number of inherited defects of amino acid metabolism in which there is a deficiency or absence of pigment in the eyes, skin, or hair.
A form of gene interaction whereby the expression of one gene interferes with or masks the expression of a different gene or genes. Genes whose expression interferes with or masks the effects of other genes are said to be epistatic to the effected genes. Genes whose expression is affected (blocked or masked) are hypostatic to the interfering genes.
An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC 1.1.1.21.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.

Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes. (1/177)

Membrane traffic between the endoplasmic reticulum (ER) and the Golgi complex is regulated by two vesicular coat complexes, COPII and COPI. COPII has been implicated in the selective packaging of anterograde cargo into coated transport vesicles budding from the ER [1]. In mammalian cells, these vesicles coalesce to form tubulo-vesicular transport complexes (TCs), which shuttle anterograde cargo from the ER to the Golgi complex [2] [3] [4]. In contrast, COPI-coated vesicles are proposed to mediate recycling of proteins from the Golgi complex to the ER [1] [5] [6] [7]. The binding of COPI to COPII-coated TCs [3] [8] [9], however, has led to the proposal that COPI binds to TCs and specifically packages recycling proteins into retrograde vesicles for return to the ER [3] [9]. To test this hypothesis, we tracked fluorescently tagged COPI and anterograde-transport markers simultaneously in living cells. COPI predominated on TCs shuttling anterograde cargo to the Golgi complex and was rarely observed on structures moving in directions consistent with retrograde transport. Furthermore, a progressive segregation of COPI-rich domains and anterograde-cargo-rich domains was observed in the TCs. This segregation and the directed motility of COPI-containing TCs were inhibited by antibodies that blocked COPI function. These observations, which are consistent with previous biochemical data [2] [9], suggest a role for COPI within TCs en route to the Golgi complex. By sequestering retrograde cargo in the anterograde-directed TCs, COPI couples the sorting of ER recycling proteins [10] to the transport of anterograde cargo.  (+info)

GTP hydrolysis by arf-1 mediates sorting and concentration of Golgi resident enzymes into functional COP I vesicles. (2/177)

Upon addition of GTPgammaS to in vitro budding reactions, COP I vesicles form but retain their coat, making them easy to isolate and analyze. We have developed an in vitro budding assay that reconstitutes the formation of COP I-derived vesicles under conditions where GTP hydrolysis can occur. Once formed, vesicles are uncoated and appear functional as they fuse readily with acceptor membranes. Electron microscopy shows a homogeneous population of uncoated vesicles that contain the medial/trans Golgi enzyme alpha1, 2-mannosidase II. Biochemical quantitation of vesicles reveals that resident Golgi enzymes are up to 10-fold more concentrated than in donor membranes, but vesicles formed in the presence of GTPgammaS show an average density of resident Golgi enzymes similar to that seen in donor membranes. We show that the sorting process is mediated by the small GTPase arf-1 as addition of a dominant, hydrolysis-deficient arf-1 (Q)71(L) mutant produced results similar to that of GTPgammaS. Strikingly, the average density of the anterograde cargo protein, polymeric IgA receptor, in COP I-derived vesicles was similar to that found in starting membranes and was independent of GTP hydrolysis. We conclude that hydrolysis of GTP bound to arf-1 promotes selective segregation and concentration of Golgi resident enzymes into COP I vesicles.  (+info)

Studies on the inhibition of endosome fusion by GTPgammaS-bound ARF. (3/177)

Using a cell free assay, we have previously shown that ARF is not required for endosome fusion but that inhibition of fusion by GTPgammaS is dependent on a cytosolic pool of ARFs. Since ARF is proposed to function in intracellular membrane traffic by promoting vesicle biogenesis, and components of clathrin- and COP-coated vesicles have been localized on endosomal structures, we investigated whether ARF-mediated inhibition of early endosome fusion involves the recruitment or irreversible association of these proteins onto endosomal membranes. We now report that depletion of components of clathrin coated vesicles (clathrin, AP-1 and AP-2) or COPI vesicles (beta COP) does not affect the capacity of GTPgammaS-activated ARF to inhibit endosome fusion. Inhibition of fusion by activated ARF is also independent of endosomal acidification since assays performed in the presence of the vacuolar ATPase inhibitor bafilomycin A1 are equally sensitive to GTPgammaS-bound ARF. Finally, in contrast to reported effects on lysosomes, we demonstrate that ARF-GTPgammaS does not induce endosomal lysis. These combined data argue that sequestration of known coat proteins to membranes by activated ARF is not involved in the inhibition of early endosome fusion and that its capacity to inhibit fusion involves other specific interactions with the endosome surface. These results contrast with the mechanistic action of ARF on intra-Golgi transport and nuclear envelope assembly.  (+info)

Mutation of the yeast epsilon-COP gene ANU2 causes abnormal nuclear morphology and defects in intracellular vesicular transport. (4/177)

Previously we reported an original method of visualizing the shape of yeast nuclei by the expression of green fluorescent protein (GFP)-tagged Xenopus nucleoplasmin in Saccharomyces cerevisiae. To identify components that determine nuclear structure, we searched for mutants exhibiting abnormal nuclear morphology from a collection of temperature-sensitive yeast strains expressing GFP-tagged nucleoplasmin. Four anu mutant strains (anu1-1, 2-1, 3-1 and 4-1; ANU=abnormal nuclear morphology) that exhibited strikingly different nuclear morphologies at the restrictive temperature as compared to the wild-type were isolated. The nuclei of these mutants were irregularly shaped and often consisted of multiple lobes. ANU1, 3 and 4 were found to encode known factors Sec24p, Sec13p and Sec18p, respectively, all of which are involved in the formation or fusion of intracellular membrane vesicles of protein transport between the endoplasmic reticulum (ER) and the Golgi apparatus. On the other hand, ANU2 was not well characterized. Disruption of ANU2 (delta anu2) was not lethal but conferred temperature-sensitivity for growth. Electron microscopic analysis of anu2-1 cells revealed not only the abnormal nuclear morphology but also excessive accumulation of ER membranes. In addition, both anu2-1 and delta anu2 cells were defective in protein transport between the ER and the Golgi, suggesting that Anu2p has an important role in vesicular transport in the early secretory pathway. Here we show that ANU2 encodes a 34 kDa polypeptide, which shares a 20% sequence identity with the mammalian epsilon-COP. Our results suggest that Anu2p is the yeast homologue of mammalian epsilon-COP and the abrupt accumulation of the ER membrane caused by a blockage of the early protein transport pathway leads to alteration of nuclear morphology of the budding yeast cells.  (+info)

The sorting determinant guiding Hsp150 to the COPI-independent transport pathway in yeast. (5/177)

The COPI coatomer is thought to be required in yeast directly for retrograde transport from the Golgi to the endoplasmic reticulum (ER), and directly or indirectly for ER-to-Golgi transport. Unexpectedly, the secretory glycoproteins Hsp150 and invertase have been found not to require COPI for ER exit. The features according to which cargo proteins are selected for the COPI-independent pathway are not known. The ER form of Hsp150 has three distinct domains: an N-terminal fragment of 54 amino acids (subunit I) is followed by 11 repeats of a 19 amino acid peptide plus a unique C-terminal fragment of 114 amino acids (subunit II). By fusing heterologous proteins to different Hsp150 domains and expressing them in sec21-1 and sec21-3 mutants with temperature-sensitive mutations in the gamma-COPI subunit, we show here that the repeats of subunit II function as sorting determinants for COPI-independent ER exit. The C-terminal fragment of Hsp150 could be replaced by E. coli beta-lactamase or rat nerve growth factor receptor ectodomain (NGFRe), and subunit I could be deleted, without inhibiting COPI-independent transport. However, when the repetitive region was omitted and beta-lactamase was fused directly to the C terminus of subunit I, COPI was required for efficient ER exit. Mass spectroscopic analysis demonstrated that both subunit I and II of Hsp150 were extensively O-glycosylated, suggesting that the O-glycosylation pattern was not decisive for cargo selection.  (+info)

Membrane flow through the Golgi apparatus: specific disassembly of the cis-Golgi network by ATP depletion. (6/177)

Incubation of NRK cells for 30 to 45 minutes with 50 mM 2-deoxy-D-glucose (DOG) in glucose and pyruvate-free medium results in depletion of the cellular ATP pool and in specific disassembly of the cis-Golgi network (CGN), with the stack of Golgi cisternae (SGC) and the trans-Golgi network (TGN) remaining intact and sensitive to BFA. The disassembly of the CGN is mediated by long tubular structures extending outwards from the Golgi complex and involves microtubules. Upon removal of DOG and addition of glucose and pyruvate to the culture medium, the morphology of the CGN is slowly reestablished. Reconstruction of the CGN involves COPI/COPII-positive vesicles that resume the transport of proteins and in particular of CGN membrane proteins out of the ER. Exit of CGN membrane proteins from the ER is insensitive to BFA. In cells pretreated with nocodazole, the CGN membrane proteins are transported to the vicinity of the SGC fragments dispersed throughout the cytoplasm. Ultrastructural studies of cells engaged in the reconstruction of the CGN revealed that the CGN cisterna emerge as tubular structures extending from 0.2-0.3 microm uncoated vesicles prior to their organization on the cis-side of the SGC.  (+info)

Yeast ER-Golgi v-SNAREs Bos1p and Bet1p differ in steady-state localization and targeting. (7/177)

Vesicle specific SNAP receptors (v-SNAREs) Bos1p and Bet1p are involved in targeting of anterograde vesicles between the endoplasmic reticulum (ER) and early Golgi of Saccharomyces cerevisiae. To analyze factors that influence the targeting of these proteins, alpha-factor tagged versions of Bos1p and Bet1p were employed. The alpha-factor can be cleaved off by the Kex2p protease as soon as the hybrid proteins reach the late Golgi compartment. The data obtained by monitoring of Kex2p cleavage, by immunofluorescence microscopy and cell fractionation showed that Bos1-alpha and Bet1-alpha have different cellular localization and dynamics. Bos1-alpha is an ER protein, which recycles between the Golgi and the ER in COPI-dependent manner. Bet1-alpha is an early Golgi protein and it does not change its localization under conditions when other recycling Golgi proteins can be trapped in the ER.  (+info)

gamma2-COP, a novel imprinted gene on chromosome 7q32, defines a new imprinting cluster in the human genome. (8/177)

We describe a novel imprinted gene, gamma 2-COP (nonclathrincoatprotein), identified in a search for expressed sequences in human chromosome 7q32 where the paternally expressed MEST gene is located. gamma 2-COP contains 24 exons and spans >50 kb of genomic DNA. Like MEST, gamma 2-COP is ubiquitously transcribed in fetal and adult tissues. In fetal tissues, including skeletal muscle, skin, kidney, adrenal, placenta, intestine, lung, chorionic plate and amnion, gamma 2-COP is imprinted and expressed from the paternal allele. In contrast to the monoallelic expression observed in these fetal tissues, biallelic expression was evident in fetal brain and liver and in adult peripheral blood. Biallelic expression in blood is supported by the demonstration of gamma 2-COP transcripts in lymphoblastoid cell lines with maternal uniparental disomy 7. Absence of paternal gamma 2-COP transcripts during embryonic development may contribute to Silver-Russell syndrome. However, on mutation scanning the only gamma 2-COP mutation detected was maternally derived. Amino acid comparison of gamma2-COP protein revealed close relation to gamma-COP, a subunit of the coatomer complex COPI, suggesting a role of gamma2-COP in cellular vesicle traffic. The existence of distinct coatomer complexes could be the basis for the functional heterogeneity of COPI vesicles in retrograde and anterograde transport and/or in cargo selection. Together, gamma 2-COP and MEST constitute a novel imprinting cluster in the human genome that may contain other, as yet unknown, imprinted genes.  (+info)

Coat protein complex I (COPI) vesicles are involved in transport processes within the early secretory pathway (Bethune et al., 2006). For their biogenesis, the small GTPase ADP ribosylation factor 1 (Arf1) in its GDP-bound form is recruited to the Golgi membrane by dimeric transmembrane proteins of the p24 family (Gommel et al., 2001) or by interaction with membrin (Honda et al., 2005). The membrane-associated Arf guanine nucleotide exchange factor GBF1 catalyzes exchange of the bound GDP to GTP (Zhao et al., 2006). Arf1-GTP dissociates from the p24 proteins and is inserted into the Golgi membrane (Franco et al., 1996; Antonny et al., 1997) as a dimer (Beck et al., 2008) to recruit the heptameric protein complex coatomer (Palmer et al., 1993). Coatomer polymerization leads to the formation of a COPI-coated vesicle (Bremser et al., 1999; Reinhard et al., 1999). Arf GTPase-activating proteins (GAPs) catalyze hydrolysis of the GTP bound to Arf1 followed by dissociation of the coat (Tanigawa et al., ...
Lipid droplets are ubiquitous triglyceride and sterol ester storage organelles required for energy storage homeostasis and biosynthesis. Although little is known about lipid droplet formation and regulation, it is clear that members of the PAT (perilipin, adipocyte differentiation related protein, tail interacting protein of 47 kDa) protein family coat the droplet surface and mediate interactions with lipases that remobilize the stored lipids. We identified key Drosophila candidate genes for lipid droplet regulation by RNA interference (RNAi) screening with an image segmentation-based optical read-out system, and show that these regulatory functions are conserved in the mouse. Those include the vesicle-mediated Coat Protein Complex I (COPI) transport complex, which is required for limiting lipid storage. We found that COPI components regulate the PAT protein composition at the lipid droplet surface, and promote the association of adipocyte triglyceride lipase (ATGL) with the lipid droplet ...
Alzheimers disease (AD) is the most common neurodegenerative disease in the elderly and the leading cause of dementia in humans. Evidence shows that cellular trafficking and recycling machineries are associated with AD risk. A recent study found that the coat protein complex I (COPI)-dependent trafficking in vivo could significantly reduce amyloid plaques in the cortex and hippocampus of neurological in the AD mouse models and identified 12 single-nucleotide polymorphisms in COPI genes to be significantly associated with increased AD risk using 6,795 samples. Here, we used a large-scale GWAS dataset to investigate the potential association between the COPI genes and AD susceptibility by both SNP and gene-based tests. The results showed that only rs9898218 was associated with AD risk with P = 0.017. We further conducted an expression quantitative trait loci (eQTLs) analysis and found that rs9898218 G allele was associated with increased COPZ2 expression in cerebellar cortex with P = 0.0184. Importantly,
Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics. The ARF1 and SAR1 GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. ARF1 has been shown to play a critical role in COPI (Coat Protein Complex I)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular COPII-mediated protein trafficking from the ER to the Golgi apparatus. This review offers a summary of vesicular trafficking with an emphasis on the ARF1 and SAR1 expression patterns at early growth stages and in the de-etiolation process.
p,Coat protein I (COPI)-coated vesicles mediate retrograde transport from the Golgi to the endoplasmic reticulum (ER), as well as transport within the Golgi. Major progress has been made in defining the structure of COPI coats, in vitro and in vivo, at resolutions as high as 9 Å. Nevertheless, important questions remain unanswered, including what specific interactions stabilize COPI coats, how COPI vesicles recognize their target membranes, and how coat disassembly is coordinated with vesicle fusion and cargo delivery. Here, we use X-ray crystallography to identify a conserved site on the COPI subunit α-COP that binds to flexible, acidic sequences containing a single tryptophan residue. One such sequence, found within α-COP itself, mediates α-COP homo-oligomerization. Another such sequence is contained within the lasso of the ER-resident Dsl1 complex, where it helps mediate the tethering of Golgi-derived COPI vesicles at the ER membrane. Together, our findings suggest that α-COP ...
SCYL1 binds COP1 vesicles that mediate retrograde Golgi-to ER transport, through an SCYL1-specific RKLD motif at the extreme C terminus [2]. Knockdown of SCYL1 disrupts Golgi morphology and blocks retrograte COPI-mediated transport from Golgi to ER [3]. The Golgi-localized Gorab protein (aka NTKL-BP1, SCYL-BP1) was found as a interactor of mouse Scyl1 by Y2H and coIP [4]. The yeast SCYL1, Cex1, also has several trafficking-associated physical and genetic interactors, including YPT6 (Golgi fusion of late endosome vesicles), COG5 and COG6 (fusion of vesicles to Golgi), several COPI complex members (COP1, SEC27, SEC29, RET2, UBP5 and BRE5 (ER-Golgi transport), and RGP1 and RIC1 (Golgi-to-ER transport) (BioGrid). SCYL2 appears to act a a different point in trafficking - the endocytosis and trafficking of surface proteins. Human SCYL2 (aka CVAK104) binds clathrin and the plasma membrane adaptor complex, AP2 [5]. Yeast SCYL2 (Cex1) was also found in a genetic screen for modifiers of a clathrin mutant ...
Microinjection of the slowly hydrolyzable GTP analogue GTP(gamma)S or the ectopic expression of a GTP restricted mutant of the small GTPase arf1 (arf1[Q71L]) leads to the rapid accumulation of COPI coated vesicles and buds in living cells. This effect is blocked at 15 degrees C and by microinjection of antibodies against (beta)-COP. Anterograde and retrograde membrane protein transport markers, which have been previously shown to be incorporated into COPI vesicles between the endoplasmic reticulum and Golgi complex, are depleted from the GTP(gamma)S or arf1[Q71L] induced COPI coated vesicles and buds. In contrast, in control cells 30 to 60% of the COPI carriers co-localize with these markers. These in vivo data corroborate recent in vitro work, suggesting that GTP(gamma)S and arf1[Q71L] interfere with the sorting of membrane proteins into Golgi derived COPI vesicles, and provide the first in vivo evidence for a role of GTP hydrolysis by arf1 in the sorting of cargo into COPI coated vesicles and ...
Author: Rein, U. et al.; Genre: Journal Article; Published in Print: 2002-04-29; Open Access; Keywords: Arf; ARF-GAP; COPI; ER-Golgi SNAREs; protein transport|br/|; Title: ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
Angiogenesis: Growth of new blood vessels by sprouting from existing ones. Anoxia: a condition characterized by an absence of oxygen supply to an organ or a tissue Apoptosis: Form of cell death, also known as programmed cell death, in which a suicide program is activated within the cell, leading to fragmentation of the DNA, shrinkage of the cytoplasm, membrane changes and cell death without lysis or damage to neighboring cells. It is a normal phenomenon, occurring frequently in a multicellular organism. ARF: ADP Ribosylation Factor (ARF) is a member of the GTP-binding proteins responsible for regulating both COPI coat assembly and clathrin coat assembly at Golgi membranes. ATM: a protein that regulates several cellular responses to DNA breaks. C. elegans: Caenorhabditis elegans is a nematode (unsegmented) worm with very simple anatomy. Chaperone (molecular chaperone): Protein that helps other proteins avoid misfolding pathways that produce inactive or aggregated polypeptides. Drosophila: ...
Vesicular transport shuttles proteins and membranes among the different organellar compartments within the cell. Coat proteins act as the core machinery that in...
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In addition to the better characterized COPI-dependent retrograde Golgi-to-ER pathway, a second COPI-independent pathway has also been identified. This pathway is RAB6 dependent and transports cargo such as glycosylation enzymes and Shiga and Shiga-like toxin through tubular carriers rather than vesicles (White et al, 1999; Girod et al, 1999; reviewed in Heffernan and Simpson, 2014). In the absence of a COPI coat, the membrane curvature necessary to initiate tubulation may be provided through the action of phospholipase A, which hydrolyzes phospholipids at the sn2 position to yield lysophospholipids. This activity is countered by lysophospholipid acyltransferases, and the balance of these may influence whether transport tubules or transport vesicles form (de Figuiredo et al, 1998; reviewed in Bechler et al, 2012). RAB6-dependent tubules also depend on the dynein-dynactin motor complex and the hoomodimeric Bicaudal proteins (Matanis et al, 2002; Yamada et al, 2013; reviewed in Heffernan and ...
ADP-Ribosylation Factor 1 is involved in regulating intracellular transport by modulating the interaction of Coat Proteins with Organelle Membranes in the early Secretory Pathway. It is a component of Coat Protein Complex I. This enzyme was formerly listed as EC 3.6.1.47 ...
TY - JOUR. T1 - Tethering assays for COPI vesicles mediated by golgins. AU - Satoh, Ayano. AU - Malsam, Jörg. AU - Warren, Graham. N1 - Funding Information: We thank all members of the Warren, Mellman, and Toomre laboratories for helpful comments and discussions, and Marino Zerial for generous provision of purified EEA1. This work was supported by the NIH and the Ludwig Institute for Cancer Research. A.S. was supported by the American Heart Association.. PY - 2005. Y1 - 2005. N2 - A method is described that allows the attachment of COPI vesicles and Golgi membranes to glass slides that can then be analyzed using electron microscopy (EM) and immuno-EM methods. Subpopulations of COPI vesicles can be bound selectively using recombinant golgins. Alternatively, COPI vesicles can be attached to prebound Golgi membranes. Marking these vesicles selectively with biotin allows their site of attachment to be identified.. AB - A method is described that allows the attachment of COPI vesicles and Golgi ...
Cytokinesis is the final step of cell division, and results from the constriction of a contractile ring comprising F-actin and myosin fibers (Satterwhite and Pollard, 1992). Microtubule bundles known as the central spindle help position the actomyosin ring at the equator (Glotzer, 2001; Cao and Wang, 1996; Inoue et al., 2004). A protein complex called centralspindlin plays a key role in initiating contractile ring formation (DAvino et al., 2005; Mishima and Glotzer, 2003). Completion of cytokinesis is dependent not only on contractile ring formation, but also on vesicle transport (Glotzer, 2001; Albertson et al., 2005; Montagnac et al., 2008; Prekeris and Gould, 2008).. The delivery of membrane components to the cleavage furrow region of the equatorial plasma membrane is thought to involve two different vesicle transport pathways: the secretory pathway and the endocytic pathway. The Drosophila melanogaster secretory pathway involves several transport proteins. Syntaxin 5 (one of the SNAREs ...
Biochemical and structural studies of eukaryotic protein complexes involved in the transport of lipids and proteins across membranes. Subcloning of genes for protein expression in bacterial and yeast expression vectors. Site-directed mutagenesis. Protein expression in Escherichia coli and Saccharomyces cerevisiae. Protein purification by affinity chromatography, ion-exchange and size-exclusion chromatograhy. Protein characterization. Protein crystallization for 3D structure determination by X-ray crystallography. The protein complexes I am studying are linked to diseases.. ...
COPE Full-Length MS Protein Standard (NP_009194), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles. It is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Coatomer complex consists of at least the alpha, beta, beta, gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding different isoforms have been identified.
Oxidative Phosphorylation: The process starts when electron carriers NADH and FADH2 unload electrons slowly into the electron transport chain (ETC), which creates energy. As electrons flow down the ETC, they meet up with oxygen to form water and CO2 as byproducts. At the same time, hydrogen ions (H+) are released as NADH & FADH2 are oxidized. H+ ions are then pumped upstream through protein complexes I, III, & IV into the intermembrane, where they build up. As they begin to gather, potential energy is created in the form of a gradient. Those ions then flow downstream through an enzyme called ATP synthase, where they re-enter the matrix as ATP molecules ...
The COPI is a comprehensive oral proficiency assessment that provides reliable, valid results to help inform instruction and gauge student progress.. The COPI is designed to assess the oral proficiency of upper high school students, college students, and professionals who are native or near-native English speakers learning the target language. The COPI provides language professionals with a computerized, time-efficient tool to assess their students language proficiency. The COPIs computerized delivery uses up-to-date technology, and its semi-adaptive design adjusts test difficulty level to students proficiency levels. Performance on the COPI is rated according to the ACTFL Proficiency Guidelines-Speaking.. The COPI is available in two formats (USB or CD) and includes the following components:. COPI Test Administration Program ...
ARF GAP Lis a kind of important regulator of introcellular transport. Recently, a novel human gene has been found from a cDNA library of second trimester human fetal liver. The amino acid sequence encoded by the novel gene has 32% similarity to rat ARF1 GAP, was thus termed as ARFGAP3. Functional studies of the new gene were performed. The full-length cDNA of ARFGAP3 was amplified from the human total placenta RNA by RT-PCR technique, then subcloned into pGEM-T vector and sequenced. The RNA Master blot and multiple tissue Northern blot analysis were used to define the expression profile and the transcript size of ARFGAP3 in human tissues. It was shown that ARFGAP3 was strongly expressed in glands and testis and that ARFGAP3 mRNA existed as only one kind of transcript of 2.7 kb in various human tissues. Then, the expression and purification of the recombinant human ARFGAP3 (rhARFGAP3) were performed. It was demonstrated that rhARFGAP3 exhibited strong GTPase-activating protein ( GAP) activity ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Jain Goyal, M., Zhao, X., Bozhinova, M., Andrade-López, K., de Heus, C., Schulze-Dramac, S., Müller-McNicoll, M., Klumperman, J. and Béthune, J. (2020) A paralog-specific role of COPI vesicles in the neuronal differentiation of mouse pluripotent cells. Life Science Alliance, 3, e202000714.. Rafiee, M.R., Sigismondo, G., Kalxdorf, M., Forster, L., Brugger, B., Béthune, J. and Krijgsveld, J. (2020) Protease-resistant streptavidin for interaction proteomics. Molecular systems biology, 16, e9370.. Adolf, F., Rhiel, M., Hessling, B., Gao, Q., Hellwig, A., Béthune, J. and Wieland, F.T. (2019) Proteomic Profiling of Mammalian COPII and COPI Vesicles. Cell reports, 26, 250-265 e255.. Béthune, J., Jansen, R.P., Feldbrugge, M. and Zarnack, K. (2019) Membrane-Associated RNA-Binding Proteins Orchestrate Organelle-Coupled Translation. Trends in cell biology, 29, 178-188.. Egetemaier, S. and Béthune, J. (2019). Proteomik-Analyse von dynamischen Proteinkomplexen. Biospektrum (Springer Verlag) 01.19, ...
COPB antibody [maD] (coatomer protein complex subunit beta 1) for ELISA, ICC/IF, WB. Anti-COPB mAb (GTX26323) is tested in Human, Monkey, Rat, Hamster samples. 100% Ab-Assurance.
Compare small ArfGAP 1 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
Plasmid pDONR223-SCYL2 from Dr. William Hahns lab contains the insert SCYL2 and is published in Nature. 2010 Nov 24. ():. This plasmid is available through Addgene.
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
This study shows a critical role for Asna1 in ensuring β-cell function. Loss of Asna1 in β-cells of mice results in pancreatic hypoinsulinemia, impaired insulin secretion, and early onset diabetes. Additionally, β-cells of Asna1β−/− mice showed impaired PM-to-TGN as well as Golgi-to-ER retrograde transport, ER stress, and mislocalization of Stx5 and Stx6. Of note, we also show that inhibition of retrograde transport at the level of EE-to-TGN in isolated islet and insulinoma cells results in impaired Golgi-to-ER retrograde transport, decreased insulin content, and ER stress. Thus, the findings provide evidence that Asna1 is required in β-cells to ensure retrograde transport, which in turn appears to be essential for ER homeostasis and proinsulin biogenesis. Additionally, the perturbed Golgi-to-ER retrograde transport in Retro-2-treated primary islets suggests that the impairment of this step in Asna1β−/− β-cells likely is secondary to the inhibition of retrograde transport at the ...
Membrane, Proteins, Endoplasmic Reticulum, Reticulum, Secretory Pathway, Yeast, Gtpase, Coated Vesicles, Copi, Copi-coated Vesicles, and Clathrin
Pasul 1. Aprinzi cuptorul, speli cartofii cu apă călduţă (nu îi cureţi de coajă), îi ştergi de apă, îi înţepi pe fiecare în parte în două locuri (opuse) cu o furculiţă, îi pui pe o coală de hârtie de copt, pe o tavă nu prea adâncă şi îi pui la cuptor, la foc puternic, vreo 15 minute şi la foc mediu spre mic până sunt gata. Când sunt gata? Atunci când sunt pătrunşi în momentul în care îi verifici cu furculiţa.. Pasul 2. În paralel, pui ouăle la fiert.. Pasul 3. Cât s-au copt cartofii şi au fiert ouăle, pregăteşti celelalte ingrediente. Adică: cureţi ceapa roşie şi ceapa verde, speli puţin măslinele de urmele de zeamă în care fuseseră murate, fărâmi telemeaua de capră şi toci cele două feluri de ceapă. Pe cea roşie - rondele, iar pe cea verde - mărunţel.. Pasul 4. După ce s-au copt, laşi cartofii să se răcorească puţin, îi tai repede în jumătăţi sau în sferturi, după cât de mari sunt. Îi stropeşti imediat cu două-trei ...
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Kei Ochiai is a rag-and-bone man for the Kanto region. He drives his small truck through neighborhoods in Tokyo and Yokohama, circling the areas while soun
Reviews of Kei Mouth by those whove been before you. Learn about Kei Mouth from other travellers. Unbiased, traveller reviews of Kei Mouth, Eastern ...
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Recently, Lanoix et al. 1999 have analyzed the resident protein (glycosyltransferase) content of an uncoated membrane fraction produced from Golgi membranes in vitro (in the presence of GTP) that is thought to be derived from COPI-coated vesicles, and compared this with bona fide COPI-coated vesicles prepared with GTPγS. They report (Table IV in Lanoix et al., 1999) a 9.6-fold higher concentration (protein/phospholipid) of NAGT I and a 4.8-fold higher concentration of Man II, in the uncoated (GTP) vesicles than in the starting Golgi fraction and an exclusion of residents in the GTPγS -prepared coated vesicles. There was no corresponding enrichment in anterograde-directed cargo in the GTP-produced uncoated vesicles (1.7-fold for pIgR) or in bona fide COP I-coated vesicles made with GTPγS (1.2-fold). In contradiction to this, Nickel et al. 1998 analyzed bona fide coated COPI vesicles produced in the presence of GTP versus GTPγS, and report that anterograde-directed cargo is up to 50-fold more ...
Coatomer subunit beta-1; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (948 aa ...
Calcium-regulated non-lysosomal thiol-protease. Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. Proteolytically cleaves the beta-subunit of coatomer complex (By similarity ...
Expression of ARFGAP2 (FLJ14576, IRZ, Zfp289, ZNF289) in nasopharynx tissue. Antibody staining with HPA016649 and HPA018152 in immunohistochemistry.
Expression of ARFGAP2 (FLJ14576, IRZ, Zfp289, ZNF289) in epididymis tissue. Antibody staining with HPA016649 and HPA018152 in immunohistochemistry.
E rawa ni da kaya ni tolu ga na domo ena vakatara: O koya e laga, o koya e tagica kei ira na droku. E na so tale na gauna e rawa ni dua e laga muria se camana. E na vakayagataki na lali me vakatautaki kina na kena gedei kei na kena totolo na i lagalaga ni meke, muria yani na derua kei na i cobo me lutu bi vinaka kina na kena i rogorogo ni vakatara. E rawa tale ga me curu mai e so na rorogo me vaka na sau me dua toka ga kei na dua na tiki ni bitu se kau me rau veiqiriti toka. Na veilutuki ni lali ka vaka kina na kena laki totolo se berabera, laki mudu vakasauri tu mada ka lako vata tiko kei na cobo kei na derua ena kuria tiko na lutu bi ni domo ni vakatara ka vakavotuya na memela vinaka ni domo ni laga ...
What the Copen lacked in horsepower, it made up with a trick metal roof that folded away into the trunk at the push of a button - if nothing was in the trunk.. Last year, Daihatsu pulled the car from the European market. By the end of this year, Daihatsu will pack up and leave the Continent completely.. At home in Japan, only some 2,000 Copen found a buyer last year, bringing the total to a mere 56,000 or so.. Daihatsu will celebrate the end of the open air era with a 10th-anniversary version of the Copen. Trying to sell 500 of the special-edition kawai kei, Daihatsu will fit it with commemorative plates, leather seats and other trimmings.. The love of the Japanese for the kei car however is unbroken. Last year, more than one million mini cars were sold in Japan, for a market share of 27 percent.. ...
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Protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus involves specific uptake into coat protein complex II (COPII)-coated vesicles of secretory and of vesicle targeting (v-SNARE) proteins. Here, two ER to Golgi v-SNAREs, Bet1p and Bos1p, were shown to interact specifically with Sar1p, Sec23p, and Sec24p, components of the COPII coat, in a guanine nucleotide-dependent fashion. Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly with the COPII coat or interact indirectly by binding to Bet1p or Bos1p. The data suggest that transmembrane proteins can be taken up into COPII vesicles by direct interactions with the coat proteins and may play a structural role in the assembly of the COPII coat complex. ...
Coatomer coated (COPI) vesicles play a pivotal role for multiple membrane trafficking steps throughout the eukaryotic cell. Our focus is on betaCOP, one of the most well known components of the COPI multi-protein complex. Amino acid differences in be
On page 1029, Supek et al. illustrate how a peripheral membrane protein organizes a coat protein complex involved in secretory vesicle formation.. The protein in question, yeast Sec16p, is an ER resident required in vivo for COPII-dependent vesicle budding. In vitro, Sec16p is not necessary for budding from liposomes reconstituted with pure cytosolic COPII proteins. However, this in vitro reaction depends on a nonhydrolyzable form of GTP, probably because the COPII coat falls apart when Sar1p (the initiator of coat assembly) hydrolyzes GTP. Until now, the function of Sec16p in liposome budding could not be tested, because the protein was difficult to purify. Supek et al. report conditions that stabilize Sec16p and have purified enough protein for in vitro studies. Microsomal membranes stripped of endogenous Sec16p were stimulated in vesicle budding by the purified. protein, but only in the presence of hydrolyzable GTP. Thus, the in vivo function of Sec16p may be either to slow GTP hydrolysis ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] The protein encoded by this gene is a member of the SEC23 subfamily of the SEC23/SEC24 family. It is part of a protein complex and found in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. This protein has similarity to yeast Sec23p component of COPII. COPII is the coat protein complex responsible for vesicle budding from the ER. The encoded protein is suggested to play a role in the ER-Golgi protein trafficking. [provided by RefSeq, Jul 2008 ...
The mechanisms underlying virion formation inside the host cell are not fully understood. Viral assembly comprises the formation of the supra-molecular complex described above that, at the cell surface, propels viral budding and release. Viral genome complex formation has been reported to be fully dependent on the establishment of RNA−RNA interactions between the different vRNPs (as reviewed in Gerber et al., 2014; Giese et al., 2016; Hutchinson et al., 2010). However, IAV assembly is heavily dependent on host processes, namely for transporting components to the budzone. The transport of the viral transmembrane proteins, HA, NA and M2 to the plasma membrane occurs via the secretory pathway (Doms et al., 1993) and involves the coat protein I (Sun et al., 2013). M1 might be transported along with vRNPs (Noton et al., 2007), M2 (Chen et al., 2008) and/or lipids to the surface, but a detailed analysis of the transport of the M1 pool included in virions is still missing. In the case of vRNPs, the ...
Sequence variants and/or copy number variants (deletions/duplications) within the ARFGAP3 gene will be detected with >99% sensitivity. Variants classified as unknown significance (VUS), likely pathogenic, or pathogenic will be reported. Benign and li...
Canadas Milos Raonic failed in his bid for a third title this season, losing 7-6 (5), 3-6, 6-0 to Kei Nishikori in the final of the Japan Open on Sunday.
Dive into the research topics where Kei Fujiwara is active. These topic labels come from the works of this person. Together they form a unique fingerprint ...
Bob Coats, or as many of you know him as Los Bobbys of The Belairs Rock and Soul Ban… Janice Coats needs your support for Bobby Coats Fund for Colon Surgery
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Crystal structure of an RNA bacteriophage coat protein-operator complex The three-dimensional structures of two complexes ... "Crystal structure of an RNA bacteriophage coat protein-operator complex". Nature. 371 (6498): 623-626. Bibcode:1994Natur.371.. ... where she was the first to describe the crystal structure of an RNA aptamer-protein complex. Her research investigates the ... "Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution". Nature Structural Biology. 5 (2): 133-139. doi: ...
AP-3 complex subunit mu-1 is a protein that in humans is encoded by the AP3M1 gene. The protein encoded by this gene is the ... Odorizzi G, Cowles CR, Emr SD (1998). "The AP-3 complex: a coat of many colours". Trends Cell Biol. 8 (7): 282-8. doi:10.1016/ ... AP-3 is a heterotetrameric protein complex composed of two large subunits (delta and beta3), a medium subunit (mu3), and a ... 2000). "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based ...
COP II is a coatomer that coats the vesicles transporting proteins from the ER to the golgi complex. This pathway is referred ... The coatomer protein complex is made up of seven nonidentical protein subunits. These seven nonidentical protein subunits are ... The Sar1-GTP and Sec23-24 complex recruits another protein complex called Sec13/Sec31. This complex polymerizes to form the ... The coatomer is a protein complex that coats membrane-bound transport vesicles. Two types of coatomers are known: COPI ( ...
... protein-coated microparticles. Antibodies react to the viral protein, forming a complex. Secondary enzyme-labeled antibodies ... A plate is coated with a viral protein, such as a SARS-CoV-2 spike protein. Samples are incubated with the protein, allowing ... The antibody-protein complex can then be detected with another wash of antibodies that produce a color/fluorescent readout. ... Antigen tests look for antigen proteins from the viral surface. In the case of a coronavirus, these are usually proteins from ...
The encoded protein has similarity to yeast Sec24p component of COPII. COPII is the coat protein complex responsible for ... Protein transport protein Sec24B is a protein that in humans is encoded by the SEC24B gene. The protein encoded by this gene is ... Tang BL, Kausalya J, Low DY, Lock ML, Hong W (Jun 1999). "A family of mammalian proteins homologous to yeast Sec24p". Biochem ... Pagano A, Letourneur F, Garcia-Estefania D, Carpentier JL, Orci L, Paccaud JP (Apr 1999). "Sec24 proteins and sorting at the ...
The encoded protein has similarity to yeast Sec24p component of COPII. COPII is the coat protein complex responsible for ... Protein transport protein Sec24C is a protein that in humans is encoded by the SEC24C gene. The protein encoded by this gene is ... "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038/ ... Tang BL, Kausalya J, Low DY, Lock ML, Hong W (1999). "A family of mammalian proteins homologous to yeast Sec24p". Biochem. ...
The encoded protein has similarity to yeast Sec24p component of COPII. COPII is the coat protein complex responsible for ... Protein transport protein Sec24D is a protein that in humans is encoded by the SEC24D gene. The protein encoded by this gene is ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038 ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (5): 277-86. doi: ...
The encoded protein has similarity to yeast Sec23p component of COPII. COPII is the coat protein complex responsible for ... Protein transport protein Sec23B is a protein that in humans is encoded by the SEC23B gene. The protein encoded by this gene is ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038 ... 1999). "Sec24 proteins and sorting at the endoplasmic reticulum". J. Biol. Chem. 274 (12): 7833-40. doi:10.1074/jbc.274.12.7833 ...
... is a coatomer, a protein complex[1] that coats vesicles transporting proteins from the cis end of the Golgi complex back ... Coat proteins[edit]. Coat protein, or COPI, is an ADP ribosylation factor (ARF)-dependent protein involved in membrane traffic. ... refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of ... Coat+Protein+Complex+I at the US National Library of Medicine Medical Subject Headings (MeSH) ...
... can induce special protein complexes called metallothioneins. Medical uses of silver Antimicrobial properties of copper Nägeli ... Galvanized (zinc-coated) fittings on roofs impede the growth of algae. Copper- and zinc-treated shingles are available. Zinc ... The metals react with thiol (-SH) or amine (-NH(1,2,3)) groups of proteins, a mode of action to which microorganisms may ... complexes work by forming superficial plugs in the sweat ducts, reducing the flow of perspiration. Orthoesters of ...
... but multiple proteins of the same variety compose the protein complexes critical to the formation of the COPII coat. These coat ... refers to the specific coat protein complex that initiates the budding process. The coat consists of large protein subcomplexes ... Sar1-GTP recruits Sec23/Sec24 coat protein to form a pre-budding complex. Pre-budding complex (composed of Sar1-GTP bound with ... COPII's coat is composed of five proteins: Sar1, Sec23, Sec24, Sec13, and Sec31. These proteins dimerize to form larger protein ...
AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ... The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric ...
Once bound, they are packaged into coat protein complex I vesicles for retrograde transport to the ER. In vitro studies in ... The protein encoded by this gene was the first member of the family to be identified, and it encodes a protein structurally and ... KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 1, also known as KDELR1, is a protein which in humans ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi: ...
CP is the coat protein of LVX that forms ribonucleoprotein complexes along with TGBp1 and viral mRNA. "The nucleotide sequence ... coat protein). In the LVX sequence, there is a region between the 12 kDa ORF and the 22 kDa (coat protein) ORF that is not ... These proteins are 24 kilodaltons (kDa), 12 kDa, and 22 kDa, with the third being the coat protein, while also encoding for RNA ... of the 24 kDa protein. This sequence is also found upstream of initiation codons of coat proteins in similar viruses, most ...
... is a protein that plays a major role in the formation of coated vesicles. Clathrin was first isolated and named by ... During mitosis, clathrin binds to the spindle apparatus, in complex with two other proteins: TACC3 and ch-TOG/CKAP5. Clathrin ... Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. The endocytosis ... Clathrin has another function aside from the coating of organelles. In non-dividing cells, the formation of clathrin-coated ...
1991). "Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta- ... Waters MG, Serafini T, Rothman JE (1991). "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated ... Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene. COPI coatomer, a protein complex GRCh38: ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ...
Waters MG, Serafini T, Rothman JE (1991). "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated ... "Entrez Gene: COPG2 coatomer protein complex, subunit gamma 2". Bermak JC, Li M, Bullock C, Weingarten P, Zhou QY (Feb 2002). " ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/ ... "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three- ...
The coats on CCVs are primarily of clathrin, adaptor protein (AP) complexes, and alternative adaptors. Her working hypothesis ... She specifically works with coated vesicles. The best-characterized coated vesicles are the clathrin-coated vesicles (CCVs). ... Robinson and her lab managed to find another AP complex, AP-3, which interacts with lysosomal membrane proteins such as LAMP1. ... She eventually succeeded in purifying components of the coat that were not clathrin and are now known as adaptor proteins. ...
Each domain contained a stem-loop that can be recognized by a PP7 bacteriophage coat protein. The complex was delivered into ... Recruiting these proteins can allow studies of specific proteins' and protein complexes' effects on gene regulation and ... Direct activation: The transcription activator, VP64, is fused to the Cas9 protein, so proper targeting of the complex results ... Allows construction of Cas9 complexes with protein binding cassettes, artificial aptamers, pools of random sequences as well as ...
Seven coat proteins have been identified, and they represent subunits of a complex known as coatomer. The subunits are ... Chow VT, Quek HH (1997). "Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA and identity of the amino ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... "Entrez Gene: COPA coatomer protein complex, subunit alpha". Gerich B, Orci L, Tschochner H, Lottspeich F, Ravazzola M, Amherdt ...
AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene. The protein encoded by this gene is the ... This complex is located at the Golgi vesicle and links clathrin to receptors in coated vesicles. These vesicles are involved in ... "Entrez Gene: AP1M1 adaptor-related protein complex 1, mu 1 subunit". Hinners I, Wendler F, Fei H, Thomas L, Thomas G, Tooze SA ... Page LJ, Robinson MS (Nov 1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". The Journal ...
The AP1 complex is located at the trans-Golgi network and associates specific proteins with clathrin-coated vesicles. This ... This gene encodes a protein that interacts with the gamma subunit of AP1 clathrin-adaptor complex. ... encoded protein may act to connect the AP1 complex to other proteins. Alternatively spliced transcript variants that encode ... Synergin gamma also known as AP1 subunit gamma-binding protein 1 (AP1GBP1) is a protein that in humans is encoded by the SYNRG ...
Activated Arf1p then recruits coat protein β-COP, a subunit of the COP-I complex, to cargo-bound receptors on the membrane.[9] ... of vesicle formation results in a buildup of SNARE proteins in the Golgi which would otherwise be bound to coat protein-coated ... Coat protein recruitment is necessary for proper vesicle formation and transport. Brefeldin A reversibly inhibits the function ... The lack of active Arf1p prevents coat protein recruitment, which then ultimately induces the fusion of neighboring ER and ...
The protein encoded by this gene is part of the clathrin coat assembly complex which links clathrin to receptors in coated ... AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene. ... "Entrez Gene: AP1S1 adaptor-related protein complex 1, sigma 1 subunit". Montpetit A, Côté S, Brustein E, Drouin CA, Lapointe L ... Boehm M, Aguilar RC, Bonifacino JS (Nov 2001). "Functional and physical interactions of the adaptor protein complex AP-4 with ...
The adaptor proteins investigated work in vesicular transport in eukaryotes, particularly in cargo-selection and coat-protein ... The study found that F. alba had all five adaptor protein complexes present in its genome, whereas the kingdom Fungi only ... in 2014 traced the evolution of the five adaptor protein (AP) complexed in fungi, but also provided some insight onto Fonticula ... contained a complete set of all five adaptor protein complexes. An amoeboid trophic phase alternating with an aggregating ...
AP2 adaptor complex Vesicular transport adaptor protein Umasankar PK, Ma L, Thieman JR, Jha A, Doray B, Watkins SC, Traub LM ( ... 2014). "A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing". eLife. ... The μ homology domain of muniscins has been reported to have evolved from part of an ancient cargo adaptor protein complex ... The muniscin protein family was initially defined in 2009 as proteins having 2 homologous domains that are involved in clathrin ...
This gene encodes a subunit of the heterotetrameric coat assembly protein complex 2 (AP2), which belongs to the adaptor ... AP-2 complex subunit mu is a protein that in humans is encoded by the AP2M1 gene. ... "Entrez Gene: AP2M1 adaptor-related protein complex 2, mu 1 subunit". Follows ER, McPheat JC, Minshull C, Moore NC, Pauptit RA, ... Zhang Y, Allison JP (Aug 1997). "Interaction of CTLA-4 with AP50, a clathrin-coated pit adaptor protein". Proceedings of the ...
COPII is the coat protein complex responsible for vesicle budding from the ER. The encoded protein is suggested to play a role ... It is part of a protein complex and found in the ribosome-free transitional face of the endoplasmic reticulum (ER) and ... Palmer KJ, Konkel JE, Stephens DJ (2005). "PCTAIRE protein kinases interact directly with the COPII complex and modulate ... Sec23 homolog A (S. cerevisiae), also known as SEC23A, is a protein which in humans is encoded by the SEC23A gene. The protein ...
Coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... "Entrez Gene: COPE coatomer protein complex, subunit epsilon". Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, ... The product of this gene is an epsilon subunit of coatomer protein complex. ...
... further processed by chemical synthesis into more complex organic molecules such as proteins or cellulose, the basic structural ... Coated with small scales (thus elepidote, without such scales).. Maculate. Stained, spotted, compare immaculate.. Papillate, or ... The broad, flat leaves with complex venation of flowering plants are known as megaphylls and the species that bear them, the ... These complex systems are not used much in morphological descriptions of taxa, but have usefulness in plant identification, [24 ...
Other more complex models compensate for some of the basic model's oversights, such as multiple traits or assumptions about how ... The HBB gene encodes information to make the beta-globin subunit of hemoglobin, which is the protein red blood cells use to ... Mendel recognized that certain pea plant traits (seed coat color, flower color, and axial spots) seemed to be inherited ... Foods with high levels of protein must be avoided. These include breast milk, eggs, chicken, beef, pork, fish, nuts, and other ...
Another complex, the BRCA1-PALB2-BRCA2 complex, and the RAD51 paralogs cooperate to load RAD51 onto ssDNA coated with RPA to ... protein C-terminus binding. • protein binding. • four-way junction DNA binding. • identical protein binding. • ... macromolecular complex. Biological process. • regulation of protein phosphorylation. • strand invasion. • mitotic recombination ... The BCDX2 complex is responsible for RAD51 recruitment or stabilization at damage sites.[29] The BCDX2 complex appears to act ...
"The structure of a protein primer-polymerase complex in the initiation of genome replication". EMBO J. 25 (4): 880-8. doi: ... These acids form a pore in the cell membrane through which RNA is injected [2]. Once inside the cell, the RNA un-coats and the ... The rest of the genome encodes structural proteins at the 5' end and non-structural proteins at the 3' end in a single ... The 1A, 1B, 1C, and 1D proteins are the capsid proteins VP4, VP2, VP3, and VP1, respectively.Virus-coded proteases perform the ...
SREBP-cleavage activating protein) and Insig1. When cholesterol levels fall, Insig-1 dissociates from the SREBP-SCAP complex, ... Low-density lipoproteins are taken into the cell by LDL receptor-mediated endocytosis in clathrin-coated pits, and then ... complex spherical particles which have an exterior composed of amphiphilic proteins and lipids whose outward-facing surface is ... Sterol Regulatory Element Binding Protein 1 and 2).[10] In the presence of cholesterol, SREBP is bound to two other proteins: ...
G-protein coupled receptor activity. Cellular component. • clathrin-coated endocytic vesicle membrane. • Golgi apparatus. • ... Wnt-protein binding. • protein binding. • protein kinase binding. • ubiquitin protein ligase binding. • transmembrane signaling ... gene family encode 7-transmembrane domain proteins that are receptors for Wnt signaling proteins. The FZD5 protein is believed ... Frizzled-5 is a protein that in humans is encoded by the FZD5 gene.[5][6][7] ...
Occasionally metal or glass troughs coated with a thin layer of Teflon are used; however they are not as enduring as solid PTFE ... Harkins, W. D. (1917). The evolution of the elements and the stability of complex atoms. J. Am. Chem. Soc., 39, 856-879. ... ranging from 2D crystallization of proteins to Brewster angle microscopy. The LB trough's general objective is to study the ... To combat this, glass troughs were used for a time, with a wax coating to prevent contamination from glass pores. This was ...
I. Isolation and characterization of the protein-glycogen complex". Journal of Biological Chemistry. 245 (24): 6642-6648. PMID ... Coats WS, Browner MF, Fletterick RJ, Newgard CB (Aug 1991). "An engineered liver glycogen phosphorylase with AMP allosteric ... First, the catalytic sites are relatively buried, 15Å from the surface of the protein and from the subunit interface.[6] This ... The glycogen phosphorylase monomer is a large protein, composed of 842 amino acids with a mass of 97.434 kDa in muscle cells. ...
It is derived from the Greek roots leuk- meaning "white" and cyt- meaning "cell". The buffy coat may sometimes be green if ... These cells bind antigens presented on MHC I complex of virus-infected or tumour cells and kill them. Nearly all nucleated ... It also makes blood vessels more permeable so neutrophils and clotting proteins can get into connective tissue more easily. ... White cells are found in the buffy coat, a thin, typically white layer of nucleated cells between the sedimented red blood ...
The proteins work together to: *trigger the recruitment of inflammatory cells.. *tag pathogens for destruction by coating their ... rid the body of neutralized antigen-antibody complexes.. Elements of the complement cascade can be found in many non-mammalian ... High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nature Reviews Immunology 5''' (4) 331-342. [1 ... The cascade is composed of many plasma proteins, which are made in the liver. ...
This is done in modern cells by ribosomes, a complex of several RNA molecules known as rRNA together with many proteins. The ... and non-coding RNA without a protein coat. Compared with other infectious plant pathogens, viroids are extremely small, ranging ... "Small Cofactors May Assist Protein Emergence from RNA World: Clues from RNA-Protein Complexes". PLOS ONE. 6 (7): e22494. ... since proteins are catalysts), with the disadvantage of having to postulate the coincident formation of two complex molecules, ...
Bacteria and fungi may form complex biofilms, protecting from immune cells and proteins; biofilms are present in the chronic ... "tag" pathogens for destruction by other cells by opsonizing, or coating, the surface of the pathogen ... This leads to antiviral protein production, such as protein kinase R, which inhibits viral protein synthesis, or the 2′,5′- ... "Resistance" (R) proteins, encoded by R genes, are widely present in plants and detect pathogens. These proteins contain domains ...
A complex molecular machine, found within all living cells, that serves as the site of biological protein synthesis.. RNA. See ... coat, coating. In the context of virus capsid, may refer colloquially to the defined geometric structure of a capsid, or the ... A complex, dynamic network of interlinking protein filaments that extends from the cell nucleus to the cell membrane and which ... G protein. A family of proteins that act as molecular switches inside cells, and are implicated in transmitting signals from a ...
An autoantigen is usually a normal protein or protein complex (and sometimes DNA or RNA) that is recognized by the immune ... Antigens are usually carried by proteins and polysaccharides, and less frequently, lipids. This includes parts (coats, capsules ... Immunoglobulin-binding protein - Proteins such as protein A, protein G, and protein L that are capable of binding to antibodies ... In order to induce an immune response, it needs to be attached to a large carrier molecule such as a protein (a complex of ...
In non-persistent and semi-persistent viruses, these domains are in the coat protein and another protein known as the helper ... During this process, a 7mG-capped host mRNA is recruited by the viral transcriptase complex and subsequently cleaved by a ... In cases when there is only a single coat protein, the basic structure consists of 60 T subunits, where T is an integer. Some ... A very small number of plant viruses have, in addition to their coat proteins, a lipid envelope. This is derived from the plant ...
The gold nanoparticles facilitate the formation of a silver coating on the dye-labeled regions of DNA or RNA, allowing SERS to ... Using antibodies and gold particles this approach can quantify proteins in serum with high sensitivity and specificity.[43] ... while the chemical theory proposes the formation of charge-transfer complexes. The chemical theory applies only for species ... SERS substrates are used to detect the presence of low abundance biomolecules, and can therefore detect proteins in body fluids ...
Teeth are complex structures made of materials specific to them. They are made of a bone-like material called dentin, which is ... Saliva also contains a glycoprotein called haptocorrin which is a binding protein to vitamin B12.[17] It binds with the vitamin ... This is how gallstones form when a small piece of calcium gets coated with either cholesterol or bilirubin and the bile ... It also maintains protein metabolism in its synthesis and degradation. In lipid metabolism it synthesises cholesterol. Fats are ...
One of the best-known examples is coat color in rabbits. A rabbit's coat color is determined by a single gene that has at least ... Often, the inheritance patterns are more complex.. The F1 offspring of Mendel's pea crosses always looked like one of the two ... People with the heterozygous form of this gene produce two different forms of the protein, each with a different effect on ... In this example, coat color is indicated by B (brown, dominant) or b (white), while tail length is indicated by S (short, ...
These core proteins and vRNA form a complex that is transported into the cell nucleus, where the RNA-dependent RNA polymerase ... that produces antibodies against proteins on the viral coat which mutate less rapidly, and thus a single shot could potentially ... matrix 1 protein), M2, NS1 (non-structural protein 1), NS2 (other name is NEP, nuclear export protein), PA, PB1 (polymerase ... protein).[63] For example, the influenza A genome contains 11 genes on eight pieces of RNA, encoding for 11 proteins: ...
After IgE coat these parasites, the Fc receptor (FcɛRI) of an eosinophil will recognize IgE. Subsequently, interaction between ... Over the course of a few hours a complex forms between the antibody, target cell, and effector cell which leads to lysis of the ... Next, the NK cells which have Fc Receptors will bind to that antibody, inducing the NK cell to release proteins such as ... During replication of a virus some of the viral proteins are expressed on the cell surface membrane of the infected cell. ...
The harmful proteins are those that do not break down due to the strong bonds of the protein. IgE antibodies bind to a receptor ... Cross-linking of the IgE and Fc receptors occurs when more than one IgE-receptor complex interacts with the same allergenic ... The IgE-coated cells, at this stage, are sensitized to the allergen.[40] ... Many food allergies are caused by hypersensitivities to particular proteins in different foods. Proteins have unique properties ...
Flavoproteins of electron transport chain, including FMN in Complex I and FAD in Complex II ... Hamilton, Richart (2015). Tarascon Pocket Pharmacopoeia 2015 Deluxe Lab-Coat Edition. Jones & Bartlett Learning. p. 230. ISBN ... In whole milk, 14% of the flavins are bound noncovalently to specific proteins.[15] Egg white and egg yolk contain specialized ... Free riboflavin is naturally present in foods along with protein-bound FMN and FAD. Bovine milk contains mainly free riboflavin ...
... brucei infective to humans requires a more complex explanation. Procyclins are proteins developed in the surface coating of ... Acosta-Serrano, A.; Vassella, E.; Liniger, M.; Renggli, C. K.; Brun, R.; Roditi, I.; Englund, P. T. (2001). "The surface coat ... Tsetse fly eradication programmes are complex and logistically demanding activities and usually involve the integration of ...
... viral coat protein, a variant called E1-A226V. This mutation potentially allows the virus to multiply more easily in mosquito ... It is a member of the Semliki Forest virus complex and is closely related to Ross River virus, O'nyong'nyong virus, and Semliki ... The virus consists of four nonstructural proteins and three structural proteins.[12] The structural proteins are the capsid and ... monocyte chemoattractant protein 1 (MCP-1), monokine induced by gamma interferon (MIG), and interferon gamma-induced protein 10 ...
This can, among other things, result in the formation of complex social processes conducive to evolutionary fitness. ... such as a coat of fur, or the sense of smell. ... attempting to use a genetic basis to explain complex behaviours ... Sociobiologists responded by pointing to the complex relationship between nature and nurture. ...
Each of these antibody subtypes binds to different proteins or protein complexes within the nucleus. They are found in many ... Microscope slides are coated with HEp-2 cells and the serum is incubated with the cells. If the said and targeted antibodies ... CENP-E is a 312kDa protein from the kinesin motor protein family. CENP-F is a 367kDa protein from the nuclear matrix that ... 54kDa and 60kDa proteins and RNA. The 60kDa DNA/RNA binding protein and 52kDa T-cell regulatory protein are the best ...
... especially in the case of DNA-binding proteins.[17] A technique was published in 2005 that involved coating a magnetic bead ... Single-complex studies[edit]. Magnetic tweezers go beyond the capabilities of other single-molecule methods, however, in that ... Fibronectin is a protein that will bind to extracellular membrane proteins. This technique allows for measurements of cell ... The coating of the microbeads may also contain ligands able to attach the molecules of interest. For example, the coating may ...
Glucocorticoids play a complex regulating role in the maintenance of tight junctions. Thyroid-stimulating hormone (TSH) and ... which coats the lining of the baby's immature intestines, and helps to prevent pathogens from invading the baby's system. ... Milk protein production, symbiont populations and fecundity". Journal of Insect Physiology. 54 (8): 1236-1242. doi:10.1016/j. ... This protolacteal fluid became a complex, nutrient-rich milk which then allowed a decline in egg size by reducing the ...
... proteins and their genes must be co-located for redox regulation according to the CoRR hypothesis for the function of DNA ... The process of electroplating uses redox reactions to coat objects with a thin layer of a material, as in chrome-plated ... Electron donors can also form charge transfer complexes with electron acceptors. Reductants in chemistry are very diverse. ... A common application of cathodic protection is in galvanized steel, in which a sacrificial coating of zinc on steel parts ...
"Coat Protein Complex I" by people in Harvard Catalyst Profiles by year, and whether "Coat Protein Complex I" was a major or ... "Coat Protein Complex I" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between ... Below are the most recent publications written about "Coat Protein Complex I" by people in Profiles. ...
The crystal structure of a high affinity RNA stem-loop complexed with the bacteriophage MS2 capsid: further challenges in the ... Crystal structure of a complex between WT bacteriophage MS2 coat protein and an F5 aptamer RNA stemloop with 2aminopurine ... Coat protein A, B, C 129 Escherichia virus ms2 Gene Name(s): ... Toggle Protein Feature View. Show All Entities. Show First Few ...
Crystal structure of the COPII coat subunit, Sec24, complexed with a peptide from the SNARE protein Sed5 (yeast syntaxin-5). * ... t-SNARE complex. COPII favors Sed5 within the Sed5/Bos1/Sec22 t-SNARE complex because t-SNARE assembly removes autoinhibitory ... The COPII coat seems to be a specific conductor of the fusogenic forms of these SNAREs, suggesting how vesicle fusion ... The COPII coat buds transport vesicles from the endoplasmic reticulum that incorporate cargo and SNARE molecules. Here, we show ...
The Golgi complex is a polarized cytoplasmic organelle that is generally considered to be built up of at least three ... Coat Protein Golgi Complex Coated Vesicle Vesicular Structure Membrane Traffic These keywords were added by machine and not by ... β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular Stomatitis ... 1993) β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular ...
"Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ... Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ... Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ... Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic... Hwang, D.-J.; Tumer, N. E ...
CD28:Nef:Clathrin-coated Pit Adapter Protein Complex [plasma membrane] (Homo sapiens) ... Formation of Nef:Cd28:Clathrin-coated Pit Adapter Protein complex Stable Identifier ... Formation of Nef:Cd28:Clathrin-coated Pit Adapter Protein complex (Homo sapiens) ...
Copi-coated Vesicles, Proteins, Clathrin, Membrane, Endoplasmic Reticulum, Reticulum, and Secretory Pathway ... The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia. Abstract ... ArfGAP1 interacts with coat proteins through tryptophan-based motifs. Abstract Brown, William J. Cornell University. 09/09/2009 ... The exomer coat complex transports Fus1p to the plasma membrane via a novel plasma membrane sorting signal in yeast. Abstract ...
... a virally encoded peripheral membrane protein. Nef binds to the adaptor protein (AP) complexes of coated vesicles, inducing an ... adaptor protein complex AP-2 subunit beta. adaptor related protein complex 2 beta 1 subunit. adaptor-related protein complex 2 ... AP-2 complex subunit beta. Names. adapter-related protein complex 2 beta subunit. adapter-related protein complex 2 subunit ... AP2B1 adaptor related protein complex 2 subunit beta 1 [Homo sapiens] AP2B1 adaptor related protein complex 2 subunit beta 1 [ ...
AP-type membrane coat adaptor complex IBA Inferred from Biological aspect of Ancestor. more info ... adapter-related protein complex 5 mu subunit. adapter-related protein complex 5 subunit mu-1. adaptor related protein complex 5 ... AP5M1 adaptor related protein complex 5 subunit mu 1 [Homo sapiens] AP5M1 adaptor related protein complex 5 subunit mu 1 [Homo ... General protein information Go to the top of the page Help Preferred Names. AP-5 complex subunit mu-1. Names. AP-5 complex ...
... is mediated by the accumulation of COPII proteins such as Sar1, Sec23/24 and Sec13/31 at specialized ER export sites (ERES). ... COP-Coated Vesicles / metabolism * Cells, Cultured * Coat Protein Complex I / metabolism* * Endoplasmic Reticulum / metabolism ... Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells Plant J. 2009 Mar;57(6):963-74 ... Protein export from the endoplasmic reticulum (ER) is mediated by the accumulation of COPII proteins such as Sar1, Sec23/24 and ...
Coat protein complex I‎ (1 К, 8 В). *. ► Cofilin 1‎ (24 В) ... Protein (lb); protein (nb); Protéin (su); Protein (hif); 朊 (lzh); بروتين (ar); Protein (br); ပရိုတိန်း (my); 蛋白質 (yue); Белок ( ... प्रोटिन (dty); Prótín (is); Protein (ms); protein (tr); لحمیات (ur); Bielkovina (sk); білок (uk); 蛋白质 (zh-cn); Protein (gsw); ... protein (sco); Уураг (mn); protein (nn); ಪ್ರೋಟೀನ್ (kn); پرۆتین (ckb); protein (en); fehérje (hu); પ્રોટિન (gu); प्रोटिन (new); ...
AP-1 complex subunit gamma-1 (Adaptor protein complex AP-1 subunit gamma-1) (Adaptor-related protein complex 1 subunit gamma-1 ... Protein. Similar proteins. Species. Score. Length. Source. H3BS13. PH domain and leucine rich repeat protein phosphatase 2. ... Protein. Similar proteins. Species. Score. Length. Source. H3BS13. PH domain and leucine rich repeat protein phosphatase 2. ... Protein. Similar proteins. Species. Score. Length. Source. H3BS13. PH domain leucine-rich repeat-containing protein phosphatase ...
Reduction of protein adsorption on silica and polystyrene surfaces due to coating with Complex Coacervate Core Micelles. / ... T1 - Reduction of protein adsorption on silica and polystyrene surfaces due to coating with Complex Coacervate Core Micelles ... Reduction of protein adsorption on silica and polystyrene surfaces due to coating with Complex Coacervate Core Micelles. ... title = "Reduction of protein adsorption on silica and polystyrene surfaces due to coating with Complex Coacervate Core ...
The COPII cage: unifying principles of vesicle coat assembly. Nat Rev Mol Cell Biol 2006;7:727-738. *CrossRef, ... The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat Cell Biol 2002;4:534-539. *PubMed, ... GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex. J Cell ... STAM Adaptor Proteins Interact with COPII Complexes and Function in ER-to-Golgi Trafficking. ...
PI 4-phosphate or PI 4,5-bisphosphate is required for the binding of these proteins to liposomes. The GTP-bound form of Sar1p ... COPII vesicle formation requires only three coat assembly subunits: Sar1p, Sec13/31p, and Sec23/24p. ... and this Sar1p-Sec23/24p complex is required for the binding of Sec13/31p. Ultrastructural analysis shows that the binding of ... COPII coat proteins to liposomes results in coated patches, coated buds, and coated vesicles of 50-90 nm in diameter. Budding ...
Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 ... Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. ... Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and ... The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting ...
COPI, coat protein complex I; AP, adaptor protein; PI4 kinase, phosphatidylinositol-4-kinae; OSBP, oxysterol binding protein; ... recruit several coat complexes, including GGA1-3/clathrin, AP-1/clathrin, AP-3/clathrin, and AP-4 coats (Bonifacino and Glick, ... De Matteis, M. A., and Godi, A. (2004). Protein-lipid interactions in membrane trafficking at the Golgi complex. Biochim. ... The Arf proteins are part of a larger family that also includes the Arf-like (Arl) proteins, whose diverse functions include ...
Extensive polymorphism in the Plasmodium vivax merozoite surface coat protein MSP-3α is limited to specific domains - Volume ... Plasmodium merozoites are covered by a complex coat of surface proteins. Several of the Merozoite Surface Proteins (MSPs) that ... Extensive polymorphism in the Plasmodium vivax merozoite surface coat protein MSP-3α is limited to specific domains. * J. C. ... We present here the first survey and analysis of the polymorphism in the recently characterized P. vivax surface protein PvMSP- ...
COPI is a coatomer, a protein complex[1] that coats vesicles transporting proteins from the cis end of the Golgi complex back ... Coat proteins[edit]. Coat protein, or COPI, is an ADP ribosylation factor (ARF)-dependent protein involved in membrane traffic. ... refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of ... Coat+Protein+Complex+I at the US National Library of Medicine Medical Subject Headings (MeSH) ...
Disulfide bond formation protein (DsbA-DsbB complex). Proteins with alpha-helical transmembrane anchors[edit]. *T cell receptor ... Inovirus (filamentous phage) major coat protein. *Pilin. *Pulmonary surfactant-associated protein. *Monoamine oxidases A and B ... In humans, 27% of all proteins have been estimated to be alpha-helical membrane proteins.[5] Beta-barrel proteins are so far ... bitopic membrane protein). 2) a polytopic transmembrane α-helical protein. 3) a polytopic transmembrane β-sheet protein. The ...
Due to the special arrangement of its molecules, a new coating made of corn starch is able to repair small scratches by itself ... USTC reports diamond ring architecture of a protein complex. 20.03.2018. Just as diamond ring is needed in marriage, NuA4/Tip60 ... Jacques Côtés team reports the 4.7 Å structure of the yeast NuA4/TIP60 complex, which elucidates the detailed architecture and ... By utilizing cryo-electron microscopy (cryo-EM), CAI Gangs team provides a high-resolution view of this complex in sub- ...
Gábor Mészáros, Elisabeth Petautschnig, Hermann Schwarzenbacher, Johann Sölkner, Genomic regions influencing coat color ... The ubiquitous protein complexes AP-3, BLOC-1, and BLOC-2, which contain as subunits the products of genes defective in various ... Functional interactions between OCA2 and the protein complexes BLOC-1, BLOC-2, and AP-3 inferred from epistatic analyses of ... These observations suggest functional links between OCA2 and these three protein complexes involved in melanosome biogenesis. ...
This paper reports on a complex structural analysis of the potato virus A coat protein using a set of complementary physico- ... This paper reports on a complex structural analysis of the potato virus A coat protein using a set of complementary physico- ... potyviruses coat protein potato virus A virus-like particles physico-chemical methods small-angle X-ray scattering dextran ... Partially disordered structure in intravirus coat protein of potyvirus potato virus A. PLoS One. 8, e67830.CrossRefGoogle ...
... coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated ... which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Lysates. Multiplex Assays. By ... Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of ...
SEC24D, SEC24 homolog D, COPII coat complex component. Orthology source: HomoloGene, HGNC ... protein coding gene. Chr3:123267455-123365641 (.). 129S1/SvImJ MGP_129S1SvImJ_G0027848. protein coding gene. Chr3:125579321- ... protein coding gene. Chr3:134513041-134624279 (+). DBA/2J MGP_DBA2J_G0027665. protein coding gene. Chr3:120494287-120592440 (+) ... protein coding gene. Chr3:124466093-124566910 (+). BALB/cJ MGP_BALBcJ_G0027819. protein coding gene. Chr3:121179309-121277488 ...
SEC24B, SEC24 homolog B, COPII coat complex component. Orthology source: HomoloGene, HGNC ... protein coding gene. Chr3:129982759-130061599 (-). 129S1/SvImJ MGP_129S1SvImJ_G0027879. protein coding gene. Chr3:132690502- ... protein coding gene. Chr3:142042091-142127779 (-). DBA/2J MGP_DBA2J_G0027696. protein coding gene. Chr3:127251016-127329443 (-) ... protein coding gene. Chr3:131375471-131456018 (-). BALB/cJ MGP_BALBcJ_G0027850. protein coding gene. Chr3:127899484-127979581 ...
Protein Coding), SEC24 Homolog D, COPII Coat Complex Component, including: function, proteins, disorders, pathways, orthologs, ... The encoded protein has similarity to yeast Sec24p component of COPII. COPII is the coat protein complex responsible for ... Protein Symbol:. O94855-SC24D_HUMAN. Recommended name:. Protein transport protein Sec24D. Protein Accession:. O94855. Secondary ... Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic ...
Protein Coding), SEC24 Homolog C, COPII Coat Complex Component, including: function, proteins, disorders, pathways, orthologs, ... The encoded protein has similarity to yeast Sec24p component of COPII. COPII is the coat protein complex responsible for ... The encoded protein has similarity to yeast Sec24p component of COPII. COPII is the coat protein complex responsible for ... Protein Symbol:. P53992-SC24C_HUMAN. Recommended name:. Protein transport protein Sec24C. Protein Accession:. P53992. Secondary ...
adaptor protein complex 2. CCP. clathrin-coated pit. CLC. clathrin light chain. CME. clathrin-mediated endocytosis. DR. death ... CME is initiated when the coat-forming protein clathrin is recruited to the PM by the heterotetrameric adaptor protein complex ... GPCR-G protein-β-arrestin super-complex mediates sustained G protein signaling. Cell. 166:907-919. doi:10.1016/j.cell.2016.07. ... endosomal sorting complexes required for transport. GPCR. G protein-coupled receptor. MVB. multivesicular body. NSCLC. non- ...
She zeroed in on CA19-9, a complex sugar structure that coats many proteins but had not previously been ascribed with any ... CA19-9 is a complex sugar structure that coats proteins. Elevated levels of CA19-9 were found to cause inflammation in the ... CA19-9 is a complex sugar structure that coats proteins. Elevated levels of CA19-9 were found to cause inflammation in the ... She has focused on a potentially powerful biomarker, a chemical structure created by complex sugar molecules called CA19-9, ...
  • The COPII coat buds transport vesicles from the endoplasmic reticulum that incorporate cargo and SNARE molecules. (rcsb.org)
  • COPII selects the free v-SNARE form of Bet1 because the LxxLE sequence is sequestered in the four-helix bundle of the v-/t-SNARE complex. (rcsb.org)
  • COPII favors Sed5 within the Sed5/Bos1/Sec22 t-SNARE complex because t-SNARE assembly removes autoinhibitory contacts to expose the YNNSNPF motif. (rcsb.org)
  • The COPII coat seems to be a specific conductor of the fusogenic forms of these SNAREs, suggesting how vesicle fusion specificity may be programmed during budding. (rcsb.org)
  • Protein export from the endoplasmic reticulum (ER) is mediated by the accumulation of COPII proteins such as Sar1, Sec23/24 and Sec13/31 at specialized ER export sites (ERES). (nih.gov)
  • To correlate the distribution of the COPII coat with the dynamics of organelle movement, quantitative live-cell imaging analyses demonstrated that AtSec24 and AtSec13 maintained a constant association with Golgi-associated ERES, irrespective of their velocity. (nih.gov)
  • Additionally, the increased availability of AtSec24 affected the distribution of AtSec13, inducing recruitment of this outer COPII coat component to ERES. (nih.gov)
  • These results provide a model that, in plants, protein export from the ER occurs via sequential recruitment of inner and outer COPII components to form transport intermediates at mobile, Golgi-associated ERES. (nih.gov)
  • This type of transport [ clarification needed ] is retrograde transport , in contrast to the anterograde transport associated with the COPII protein. (wikipedia.org)
  • The encoded protein has similarity to yeast Sec24p component of COPII. (genecards.org)
  • COPII is the coat protein complex responsible for vesicle budding from the ER. (genecards.org)
  • SEC24D (SEC24 Homolog D, COPII Coat Complex Component) is a Protein Coding gene. (genecards.org)
  • Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). (genecards.org)
  • Plays a central role in cargo selection within the COPII complex and together with SEC24C may have a different specificity compared to SEC24A and SEC24B (PubMed:17499046, PubMed:20427317, PubMed:18843296). (genecards.org)
  • Coat protein complex II (COPII) proteins are enriched at tER sites, although the mechanisms underlying tER site assembly and maintenance are not understood. (pubmedcentralcanada.ca)
  • Bulk phospholipids were also required for tER site structure and function in vitro, whereas depletion of phophatidylinositol selectively inhibited coat protein complex II (COPII) budding but not assembly of tER site structures. (pubmedcentralcanada.ca)
  • COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. (pnas.org)
  • Putting together the architecture of these Sec complexes with the interactions between their subunits and the appearance of the coat in COPII-coated vesicles, we present a model for COPII coat organization. (pnas.org)
  • A group of cytosolic proteins collectively known as COPII carry out a programmed set of sequential interactions, leading to cargo sorting and vesicle budding ( 4 ). (pnas.org)
  • We know relatively little, however, about the structure and modes of association of the COPII components, as needed to explain the mechanics of coat formation and membrane budding. (pnas.org)
  • These results lead us to propose a model for assembly of a COPII coat. (pnas.org)
  • Sar1 is the small GTPase that regulates assembly of COPII (coat protein complex II) on carriers that transport secretory cargo from ER to Golgi. (deepdyve.com)
  • CDAII is caused by mutations in the SEC23B gene, which encodes a core component of the coat protein complex II (COPII). (bloodjournal.org)
  • Anderson disease or chylomicron retention disorder (CMRD), 1 a disease characterized by malabsorption of lipids from the diet and accumulation of chylomicrons in the enterocytes, results from mutations in SAR1B , a component of coat protein complex II (COPII)-coated vesicles that bud from the surface of the ER and transport cargo proteins to the Golgi apparatus. (bloodjournal.org)
  • Mutations in SEC23A , another component of the COPII coat, result in cranio-lenticulo-sutural-dysplasia (CLSD), 2 an autosomal recessive syndrome characterized by sutural cataracts, late closure of the cranial fontanelles, skeletal abnormalities, and dysmorphic facial features. (bloodjournal.org)
  • The proteins that are to be transported out of the ER are routed to ER exit sites where they are packaged into COPII-coated vesicles. (bloodjournal.org)
  • COPII coat composition and assembly has been extensively studied and well characterized in Saccharomyces cerevisiae . (bloodjournal.org)
  • 15 ⇓ - 17 The core components of the COPII coat form 2 layers: an inner layer composed of the monomeric GTP-binding protein Sar1p and the heterodimeric complex Sec23p-Sec24p, and an outer layer formed by the heterotetrameric complex Sec13p-Sec31p. (bloodjournal.org)
  • We see that these interactions occur in close proximity to COPII proteins, indicating that the complex preassembles in the endoplasmic reticulum (ER) before it is trafficked to the Golgi. (biologists.org)
  • ARF1 has been shown to play a critical role in COPI (Coat Protein Complex I)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular COPII-mediated protein trafficking from the ER to the Golgi apparatus. (mdpi.com)
  • This coat (COPII) resembles another coat complex (COPI) that creates transport vesicles within the Golgi apparatus. (berkeley.edu)
  • Our working model is that the Sec protein subunits of the COPII coat bind to the ER membrane and recruit cargo molecules into a cluster that then dimples the membrane to form a bud. (berkeley.edu)
  • A direct interaction between one of the COPII subunits, Sec24p, and membrane proteins is implicated in the capture of cargo proteins. (berkeley.edu)
  • A model for the binding of coat proteins and capture of membrane molecules in COPII vesicles. (berkeley.edu)
  • In addition to a role in cargo selection, the COPII coat is responsible for the membrane shape change that accompanies vesicle budding. (berkeley.edu)
  • Liposomes formulated with phospholipids representative of a yeast ER membrane fraction bind the COPII proteins in the same sequence of events and with the same nucleotide dependence as observed with native ER membrane. (berkeley.edu)
  • The SEC23B gene provides instructions for making one component of a large group of interacting proteins called coat protein complex II (COPII). (medlineplus.gov)
  • COPII is involved in the formation of vesicles, which are small sac-like structures that transport proteins and other materials within cells. (medlineplus.gov)
  • Specifically, COPII triggers the formation of vesicles in a cellular structure called the endoplasmic reticulum (ER), which is involved in protein processing and transport. (medlineplus.gov)
  • These COPII vesicles carry proteins that are destined to be exported out of cells (secreted). (medlineplus.gov)
  • These proteins are both components of COPII, and they appear to have overlapping functions. (medlineplus.gov)
  • Assembly, organization, and function of the COPII coat. (medlineplus.gov)
  • The Golgi complex is a polarized cytoplasmic organelle that is generally considered to be built up of at least three functionally distinct, membrane bounded subcompartments, the cis-Golgi network (CGN), the stacked Golgi cisternae and the trans-Golgi network (TGN) [Mellman and Simons, 1992]. (springer.com)
  • Duden R, Griffiths G, Frank R, Argos P, Kreis TE (1991) ß-COP, a 110kD protein associated with nonclathrin coated vesicles and cisternae of the Golgi complex shows homology to b-adaptin. (springer.com)
  • Duden R, Allan VJ, Kreis TE (1991) Involvement of 0-COP in membrane traffic through the Golgi complex. (springer.com)
  • Griffiths G, Simons K (1986) The trans Golgi network: sorting at the exit site of the Golgi complex. (springer.com)
  • Mellman I, Simons K (1992) The Golgi complex: in vitro veritas? (springer.com)
  • Kreis TE (1992) Regulation of vesicular and tubular membrane traffic of the Golgi complex by coat proteins. (springer.com)
  • Schweizer A, Fransen, JAM, Matter K, Kreis TE, Ginsel L, Hauri HP (1990) Identification of an intermediate compartment involved in protein transport from the endoplasmic reticulum to Golgi apparatus. (springer.com)
  • Serafini T, Orci L, Amherdt M, Brunner M, Kahn RA, Rothman JE (1991) ADP-ribosylation factor (ARF) is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. (springer.com)
  • Waters MG, Serafini T, Rothman JE (1991) "Coatomer": a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. (springer.com)
  • However, recruitment of AtSec24 and AtSec13 to ERES, as well as the number of ERES marked by these proteins, was influenced by export of membrane cargo proteins from the ER to the Golgi. (nih.gov)
  • Actin dynamics is a tightly regulated process involved in various cellular events including biogenesis of clathrin-coated, AP-1 (adaptor protein 1)-coated transport carriers connecting the trans-Golgi network (TGN) and the endocytic pathway. (nih.gov)
  • COPI is a coatomer , a protein complex [1] that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized , and between Golgi compartments. (wikipedia.org)
  • The name "COPI" refers to the specific coat protein complex that initiates the budding process on the cis -Golgi membrane. (wikipedia.org)
  • Luminal proteins: Proteins found in the lumen of the Golgi complex that need to be transported to the lumen of the ER contain the signal peptide KDEL . (wikipedia.org)
  • Membrane proteins: Transmembrane proteins which reside in the ER contain sorting signals in their cytosolic tails which direct the protein to exit the Golgi and return to the ER. (wikipedia.org)
  • The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. (abcam.com)
  • Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. (abcam.com)
  • the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. (abcam.com)
  • The formation of coat protein complex I (COPI)-coated vesicles is regulated by the small guanosine triphosphatase (GTPase) adenosine diphosphate ribosylation factor 1 (Arf1), which in its GTP-bound form recruits coatomer to the Golgi membrane. (rupress.org)
  • The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex (PubMed:17499046, PubMed:20427317, PubMed:18843296). (genecards.org)
  • As a generalization, class I and II Arfs mainly localize to the trans-Golgi network (TGN), endoplasmic reticulum-Golgi intermediate complex (ERGIC) and Golgi apparatus to mediate membrane trafficking between these compartments, whereas the class III Arf6 localizes to the plasma membrane and is involved in endocytosis ( 2-4 ). (bioscience.org)
  • Transport of proteins in eukaryotic cells from the endoplasmic reticulum (ER) to the Golgi complex proceeds by deformation of specialized portions of the donor membrane to form carrier vesicles ( 1 - 3 ). (pnas.org)
  • In addition to recruiting Sec23p/24p, the GTP-bound form of Sar1p stabilizes Sec23p and binds to certain ER/Golgi SNARE proteins involved in the specificity of targeting and in the fusion reaction of vesicles with acceptor membranes ( 9 ). (pnas.org)
  • Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. (abcam.com)
  • Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. (abcam.com)
  • Brandizzi, Federica 2008-03-06 00:00:00 In plants, differentiation of subdomains of the endoplasmic reticulum (ER) dedicated to protein export, the ER export sites (ERES), is influenced by the type of export-competent membrane cargo to be delivered to the Golgi. (deepdyve.com)
  • The prevailing view is that AP-2 mediates endocytosis from the plasma membrane, whereas AP-1, AP-3, and AP-4 participate in the protein sorting from the trans-Golgi network and/or endosomes to lysosomes. (jimmunol.org)
  • 14 The ER and Golgi apparatus are not only the initial stations of the secretory pathway, but also the common organelles through which all secreted proteins navigate while advancing toward their final destinations. (bloodjournal.org)
  • Some proteins stay in the ER as resident ER proteins, while the majority are transported to the Golgi apparatus for further posttranslational modification before reaching their final destinations-lysosomes, endosomes, plasma membrane, or the extracellular space. (bloodjournal.org)
  • This gene encodes a subunit of a heterotetrameric adapter-like complex 4 that is involved in targeting proteins from the trans-Golgi network to the endosomal-lysosomal system. (nih.gov)
  • AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. (nih.gov)
  • We have developed biochemical assays that measure the early events of polypeptide translocation into the endoplasmic reticulum (ER) and of vesicle-mediated protein transport from the ER to the Golgi apparatus. (berkeley.edu)
  • Little is known about the mechanism of sorting and packaging of secretory proteins that transit from the Golgi complex to the cell surface. (berkeley.edu)
  • Although some proteins use clathrin to traverse the endosome en route to the plasma membrane, others do not, and, until now, the general view has been that the direct path out of the trans-Golgi network (TGN) may involve tubular carriers formed without the intervention of coat proteins. (berkeley.edu)
  • The protein encoded by this gene is the medium subunit of AP-3, which is an adaptor-related protein complex associated with the Golgi region as well as more peripheral intracellular structures. (wikipedia.org)
  • AP-3 facilitates the budding of vesicles from the Golgi membrane and may be directly involved in protein sorting to the endosomal/lysosomal system. (wikipedia.org)
  • GTP-binding proteins involved in protein trafficking by modulating vesicle budding and uncoating within the Golgi apparatus. (ebi.ac.uk)
  • Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting. (harvard.edu)
  • Electron micrograph of in vitro-formed COPI-coated vesicles. (wikipedia.org)
  • Coat protein, or COPI, is an ADP ribosylation factor (ARF)-dependent protein involved in membrane traffic. (wikipedia.org)
  • COPI consists of seven subunits which compose the heteroheptameric protein complex. (wikipedia.org)
  • COPI-coated vesicle membrane. (abcam.com)
  • Here we show that the coat protein I (COPI) complex sorts anterograde cargoes into these tubules in human cells. (nature.com)
  • ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat. (nature.com)
  • Other coat protein complexes (clathrin and COPI) display similar budding activity on synthetic membrane liposomes. (berkeley.edu)
  • Coatomer coated (COPI) vesicles play a pivotal role for multiple membrane trafficking steps throughout the eukaryotic cell. (biomedsearch.com)
  • Our focus is on betaCOP, one of the most well known components of the COPI multi-protein complex. (biomedsearch.com)
  • Arfs affect membrane traffic in part by recruiting coat proteins, including COPI and clathrin adaptor complexes, to membranes. (sciencemag.org)
  • Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. (nih.gov)
  • The ubiquitous protein complexes AP-3, BLOC-1, and BLOC-2, which contain as subunits the products of genes defective in various types of Hermansky-Pudlak syndrome, have been likewise implicated in trafficking to melanosomes. (wiley.com)
  • We determined the roles of several B. anthracis orthologues of Bacillus subtilis coat protein genes in spore assembly and virulence. (asm.org)
  • This disorder results from mutations in either LMAN1 4 (lectin mannose-binding protein 1) or MCFD2 5 (multiple coagulation factor deficiency protein 2), 2 genes that encode the components of a specific ER cargo receptor for FV and FVIII. (bloodjournal.org)
  • The known USH genes encode proteins with diverse functions, including transmembrane adhesion and signaling, scaffolding, and myosinmotor transport. (biologists.org)
  • Our long-term goal is to identify the critical genes and cellular pathways affected by misfolded human disease proteins. (stanford.edu)
  • Genes produce Proteins, which allows your whole body to do work. (whitedust.net)
  • Schematic representation of transmembrane proteins: 1) a single transmembrane α-helix (bitopic membrane protein). (wikipedia.org)
  • Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. (wikipedia.org)
  • [1] Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-span (or bitopic ) or multi-span (polytopic). (wikipedia.org)
  • [4] This is the major category of transmembrane proteins. (wikipedia.org)
  • All beta-barrel transmembrane proteins have simplest up-and-down topology, which may reflect their common evolutionary origin and similar folding mechanism. (wikipedia.org)
  • Type I transmembrane proteins are anchored to the lipid membrane with a stop-transfer anchor sequence and have their N-terminal domains targeted to the ER lumen during synthesis (and the extracellular space, if mature forms are located on plasmalemma ). (wikipedia.org)
  • AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. (abcam.com)
  • TJs lay in the apical domain of epithelial cells and are mainly composed by transmembrane proteins such as occludin, claudins, JAMs, and tricellulin, that are associated with the cytoplasmic plaque formed by proteins from the MAGUK family, such as ZO-1/2/3, connecting TJ to the actin cytoskeleton, and cingulin and paracingulin connecting TJ to the microtubule network. (frontiersin.org)
  • Secretory proteins are exported from the endoplasmic reticulum (ER) at specialized regions known as the transitional ER (tER). (pubmedcentralcanada.ca)
  • The biogenesis of secretory proteins is initiated at the endoplasmic reticulum (ER) where nascent polypeptides are translated, folded, and then transported forward in membrane-bound carrier vesicles. (pubmedcentralcanada.ca)
  • In yeast, there are at least two vesicle populations upon ER (endoplasmic reticulum) exit, one containing Gap1p (general aminoacid permease) and a glycosylated α-factor, gpαF (glycosylated proα-factor), and the other containing GPI (glycosylphosphatidylinositol)-anchored proteins, Gas1p (glycophospholipid-anchored surface protein) and Yps1p. (biochemj.org)
  • We found that the proteins are in close enough proximity to form complexes and that these complexes preassemble at the endoplasmic reticulum (ER). (biologists.org)
  • The coat consists of large protein subcomplexes that are made of seven different protein subunits, namely α, β, β', γ, δ , ε and ζ . (wikipedia.org)
  • Prof. CAI Gang and Prof. Jacques Côté's team reports the 4.7 Å structure of the yeast NuA4/TIP60 complex, which elucidates the detailed architecture and molecular interactions between NuA4 subunits. (innovations-report.com)
  • We have demonstrated previously that this protein does not exist as individual subunits in solution and undergoes association into oligomers with subsequent transition to β‑conformation. (springer.com)
  • β-Structure of the coat protein subunits in spherical particles generated by tobacco mosaic virus thermal denaturation. (springer.com)
  • AP-3 is a heterotetrameric protein complex composed of two large subunits (delta and beta3), a medium subunit (mu3), and a small subunit (sigma 3). (wikipedia.org)
  • Large food molecules (for example, proteins, lipids, nucleic acids, and starches) must be broken down into subunits that are small enough to be absorbed by the lining of the alimentary canal. (amazonaws.com)
  • In the classical signaling paradigm, the G-protein complex consists of three different subunits, G α , G β , and G γ , which form a heterotrimeric complex. (plantphysiol.org)
  • one canonical G-protein α subunit ( GPA1 ), one G-protein β subunit ( AGB1 ), two G-protein γ subunits ( AGG1 and AGG2 ), at least one candidate GPCR ( GCR1 ), and one regulator of G-protein signaling ( RGS1 ) protein (for review, see Jones and Assmann, 2004 ). (plantphysiol.org)
  • Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. (uniprot.org)
  • ADP ribosylation factors (Arfs) constitute a family of GTP binding proteins that regulate membrane trafficking pathways. (bioscience.org)
  • Extracellular bacteria such as EPEC and EHEC living in the intestinal lumen inject effectors proteins directly from the bacterial cytoplasm to the host cell cytoplasm, where they play a relevant role in the manipulation of the eukaryotic cell functions by modifying or blocking cell signaling pathways. (frontiersin.org)
  • EPEC and EHEC secrete effectors that mimic host proteins to manipulate the signaling pathways, including those related to TJ dynamics. (frontiersin.org)
  • They control the vesicular transport of proteins in different trafficking pathways (PubMed:10066790, PubMed:10436028). (nih.gov)
  • Sorting nexins Synaptotagmin TRAPP complex Synaptophysin Auxilin There are multiple pathways, each using its own coat and GTPase. (wikipedia.org)
  • GTP-binding proteins involved in signalling pathways. (ebi.ac.uk)
  • We are now using these models to perform high-throughput genetic and small molecule screens to elucidate the molecular pathways that regulate the function of these disease proteins and control their conversion to a pathological conformation. (stanford.edu)
  • Thus, cell- and tissue-specific functional interaction in response to a given signal such as ABA may determine the distinct pathways regulated by the individual members of the G-protein complex. (plantphysiol.org)
  • For instance, issues can arise in the complex chemical pathways that generate energy in mitochondria, and mutations can occur in mitochondrial DNA. (medicalnewstoday.com)
  • Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. (uniprot.org)
  • The Rac1 GTPase and its exchange factor beta-PIX (PAK-interacting exchange factor) activate these complexes, allowing N-WASP-dependent and Arp2/3-dependent actin polymerization towards membranes, thus promoting tubule formation. (nih.gov)
  • Alpha-helical proteins are present in the inner membranes of bacterial cells or the plasma membrane of eukaryotes, and sometimes in the outer membranes . (wikipedia.org)
  • [5] Beta-barrel proteins are so far found only in outer membranes of gram-negative bacteria , cell walls of gram-positive bacteria , outer membranes of mitochondria and chloroplasts , or can be secreted as pore-forming toxins . (wikipedia.org)
  • Transmembrane α-helical proteins are unusually stable judging from thermal denaturation studies, because they do not unfold completely within the membranes (the complete unfolding would require breaking down too many α-helical H-bonds in the nonpolar media). (wikipedia.org)
  • On the other hand, these proteins easily misfold , due to non-native aggregation in membranes, transition to the molten globule states, formation of non-native disulfide bonds , or unfolding of peripheral regions and nonregular loops that are locally less stable. (wikipedia.org)
  • These proteins will support a cargo-carrying budding reaction from isolated ER membranes. (pnas.org)
  • ER membranes with Sec23p/24p and Sar1p can then recruit Sec13p/31p, a complex that is likely to act as a scaffold, like clathrin, to effect membrane deformation and vesicle budding. (pnas.org)
  • The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. (abcam.com)
  • The exomer is a large, ~1-MDa complex that binds membranes in the presence of a GTP-activated form of Arf1p, a small GTPase implicated in other coat protein assembly events. (berkeley.edu)
  • The localization of MP with ER membranes is consistent with results of several studies indicating that ER membranes act as sites for virus replication and virus protein synthesis ( 6 , 42 , 76 ). (asm.org)
  • During infection, ER membranes aggregate to form inclusions that function as virus factories ( 42 , 86 ) or virus replication complexes ( 6 ) that contain vRNA in addition to replicase and MP ( 66 ). (asm.org)
  • ADP-Ribosylation Factor 1 is involved in regulating intracellular transport by modulating the interaction of Coat Proteins with Organelle Membranes in the early Secretory Pathway . (online-medical-dictionary.org)
  • A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. (nih.gov)
  • Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. (uniprot.org)
  • AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. (uniprot.org)
  • AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. (uniprot.org)
  • The primary function of adaptors is the selection of cargo proteins for their incorporation into nascent carriers. (wikipedia.org)
  • [10] [9] The order in which adaptor proteins associate with cargo, or adaptor proteins associate with ARFs is unclear, however, in order to form a mature transport carrier coat protein, adaptor, cargo, and ARF must all associate. (wikipedia.org)
  • Arf GTPase-activating protein (GAP) catalyzed GTP hydrolysis in Arf1 triggers uncoating and is required for uptake of cargo molecules into vesicles. (rupress.org)
  • May more specifically package GPI-anchored proteins through the cargo receptor TMED10 (PubMed:20427317). (genecards.org)
  • In the case of clathrin-coated vesicles, the equivalent information for components of the clathrin coat has led to an understanding of the molecular basis for internal cargo sorting and for coat assembly ( 1 ). (pnas.org)
  • As their name implies, APs select and link specific cargo molecules to the clathrin molecules, participating in the membrane assembly of clathrin-coated pits. (jimmunol.org)
  • F5F8D results from mutations in either LMAN1 (lectin mannose-binding protein 1) or MCFD2 (multiple coagulation factor deficiency protein 2), which encode the ER cargo receptor complex LMAN1-MCFD2. (bloodjournal.org)
  • Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. (nih.gov)
  • Transport of secretory and membrane cargo proteins is mediated by diffusible vesicles. (berkeley.edu)
  • This capture results in the concentrative sorting of membrane and secretory proteins, the latter being selected by an indirect interaction mediated by various membrane receptor proteins that link the coat to soluble cargo proteins. (berkeley.edu)
  • abstract = "The thermodynamic contribution of a stacking interaction between Tyr85 in MS2 coat protein and a single-stranded pyrimidine in its RNA binding site has been examined. (northwestern.edu)
  • This protein in turn binds to the ARF. (wikipedia.org)
  • In this report we used two AP-2 complex-specific inhibitors: a dominant negative mutant of Eps15 (Eps15DIII) that binds to the α subunit of AP-2 complex and a small interference RNA that is specific for the μ2 subunit of AP-2 complex. (jimmunol.org)
  • Here, we have used a variety of in vivo and in vitro assays to determine that the MP functions as a genuine microtubule-associated protein that binds microtubules directly and modulates microtubule stability. (asm.org)
  • The MP modulates the size-exclusion limit (SEL) of the Pd ( 107 ) and also binds single-stranded nucleic acids in vitro to form an unfolded, elongated ribonucleoprotein complex with apparent dimensions compatible with translocation through dilated Pd ( 22 , 23 , 53 ). (asm.org)
  • There are 6 mammalian ARFs which are regulated by over 30 guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs). (wikipedia.org)
  • This cycle is mediated by guanine nucleotide exchange factors (GEFs) and guanine nucleotide activating proteins (GAPs) known as Arf GEFs and Arf GAPs. (bioscience.org)
  • GTPases are inactivated through either the intrinsic capability of the GTPase to hydrolyze GTP to GDP+Pi or an interaction with another protein group, the GTPase-activating proteins (GAPs). (mdpi.com)
  • The activities of some guanine nucleotide exchange factors (GEFs) and guanosine triphosphatase (GTPase)-activating proteins (GAPs) are stimulated by phosphoinositides, including phosphatidylinositol 3,4,5-trisphosphate (PIP3) and phosphatidylinositol 4,5-bisphosphate (PIP2), and phosphatidic acid (PA), likely providing both a means to respond to regulatory signals and a mechanism to coordinate GTP binding and hydrolysis. (sciencemag.org)
  • HPS-2 disease results from mutations in the b3A subunit of a coat protein, adaptor complex-3, responsible for intracellular vesicle formation. (clinicaltrials.gov)
  • For polyplexes, fibronectin fragment resulted in greater intracellular trafficking efficiency compared to PP-12 protein polymer. (pubmedcentralcanada.ca)
  • The encoded protein is found on the cytoplasmic face of coated vesicles in the plasma membrane. (nih.gov)
  • Nef induces accelerated endocytosis of CD28 via clathrin-coated pits. (reactome.org)
  • FCHo proteins are nucleators of clathrin-mediated endocytosis. (springer.com)
  • The transmitter release-site CaV2.2 channel cluster is linked to an endocytosis coat protein complex. (springer.com)
  • Upon PMA treatment, CD4 becomes localized in clathrin-coated pits, suggesting that the down-regulation is a clathrin-mediated endocytosis process ( 3 ). (jimmunol.org)
  • Endosomes (receptor-mediated endocytosis) Membrane transport protein Wikipedia:MeSH D12.776#MeSH D12.776.543.990 --- vesicular transport proteins Vesicular+Transport+Proteins at the US National Library of Medicine Medical Subject Headings (MeSH) Yasushi Sako (1 October 2010). (wikipedia.org)
  • Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). (nih.gov)
  • Thus, the ECM protein targets the vector toward a specific internalization pathway that can influence the ultimate fate of the vector, as internalization via caveolae-mediated endocytosis may avoid the lysosome and subsequent degradation relative to internalization via clathrin-mediated endocytosis 17 , 18 . (pubmedcentralcanada.ca)
  • Hence they bring their effectors, proteins that bind specifically to the GTP-bound form, into close contact with the lipid bilayer. (frontiersin.org)
  • This classification refers to the position of the protein N- and C-termini on the different sides of the lipid bilayer . (wikipedia.org)
  • The portion of the membrane proteins that are attached to the lipid bilayer (see annular lipid shell ) consist mostly of hydrophobic amino acids. (wikipedia.org)
  • The membrane system of eukaryotic cells is a complex, highly developed network of distinct compartments consisting of unique repertoires of lipid and protein composition. (bioscience.org)
  • Here, we investigated the dynamic properties of tER sites in Saccharomyces cerevisiae and probed protein and lipid requirements for tER site structure and function. (pubmedcentralcanada.ca)
  • We propose that tER site structures are stable elements that are assembled on an underlying protein and lipid scaffold. (pubmedcentralcanada.ca)
  • To gain basic insight into the protein and lipid requirements for tER site assembly, we have examined the influence of specific mutations and inhibitors on tER site structure and function in S. cerevisiae by using in vivo and cell-free approaches. (pubmedcentralcanada.ca)
  • The small packages are made of fat (lipid) on the inside and proteins on the outside. (ezsoftech.com)
  • It digests complex fat (or lipid) molecules into simple, soluble fatty acid and glycerol molecules. (amazonaws.com)
  • This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. (pnas.org)
  • Completing the cycle, Sec23p acts as a GTPase-activating protein for Sar1p ( 8 ). (pnas.org)
  • Guanine-nucleotide exchange factors (GEFs), GDP dissociation inhibitors (GDIs), and GTPase-activating proteins are regulators of small GTP-binding proteins ( Figure 1 ). (mdpi.com)
  • Small GTPase domain found in mitochondrial proteins involved in mitochondrial trafficking. (ebi.ac.uk)
  • The small GTPase-like protein LIP2 (light insensitive period 2) from Arabidopsis thaliana is implicated in control of the plant circadian rhythm [ PMID: 17683937 ]. (ebi.ac.uk)
  • Schekman R (1985) Protein localization and membrane traffic in yeast. (springer.com)
  • We investigated the molecular organization and structure of Sec23p/24p and Sec13p/31p complexes isolated from yeast cells. (pnas.org)
  • We found that mutant Gas1 proteins that lack a GPI anchor and/or S/T region (serine- and threonine-rich region), two common characteristic features conserved among yeast GPI-anchored proteins, were still sorted away from Gap1p-containing vesicles. (biochemj.org)
  • Basic principles that emerged from these studies in yeast are now being applied to studies of genetic diseases of protein transport. (berkeley.edu)
  • Protein transport in yeast appears to be mediated by the same organelles and proteins that operate in mammalian cells. (berkeley.edu)
  • mammalian equivalents of the yeast Sec proteins have been isolated and are known to operate in the same location within the cell. (berkeley.edu)
  • To examine this limb of the secretory pathway, we have examined two membrane proteins: a biosynthetic enzyme, chitin synthase III (Chs3p), and a mating cell fusion protein, Fus1p, which travel from the TGN/endosome membrane to the plasma membrane in yeast. (berkeley.edu)
  • We use the baker's yeast, Saccharomyces cerevisiae, as a model system to study the cell biology underpinning protein-misfolding diseases like Parkinson's disease and ALS. (stanford.edu)
  • Since dealing with misfolded proteins is an ancient problem, we hypothesize that the mechanisms employed to cope with them are likely conserved from yeast to man. (stanford.edu)
  • Encouraged by the power of the yeast system to gain insight into α-synuclein biology, we are creating new yeast models to study additional protein-misfolding disorders, including Alzheimer's disease and ALS. (stanford.edu)
  • We recently developed a yeast model to study the ALS disease protein TDP-43 (Johnson et al. (stanford.edu)
  • Interestingly, one of the hits from our yeast TDP-43 genetic modifier screen, PBP1, is the homolog of a human neurodegenerative disease protein, ataxin 2. (stanford.edu)
  • Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics. (mdpi.com)
  • In eukaryotic cells, small GTP-binding proteins comprise the largest family of signaling proteins. (mdpi.com)
  • Due to the special arrangement of its molecules, a new coating made of corn starch is able to repair small scratches by itself through heat: The cross-linking via ring-shaped molecules makes the material mobile, so that it compensates for the scratches and these disappear again. (innovations-report.com)
  • Denaturation of the potato virus A coat protein molecules occurs in the presence of detergent concentrations that are seven times lower than that in albumins (5.2 and 35 mM), which confirms low stability of the potato virus A coat protein. (springer.com)
  • She has focused on a potentially powerful biomarker, a chemical structure created by complex sugar molecules called CA19-9, since CA19-9 is elevated in patients with pancreatitis and pancreatic cancer. (cshl.edu)
  • A vesicular transport protein, or vesicular transporter, is a membrane protein that regulates or facilitates the movement of specific molecules across a vesicle's membrane. (wikipedia.org)
  • Proteins are long chains of amino acids, and protease enzymes break them into peptides (smaller chains of amino acids molecules) and eventually into individual amino acids, which are small and easily absorbed in the small intestine. (amazonaws.com)
  • Research of the dynamics of protein and DNA molecules will be a major research issue in our Biophysics group for years to come. (wur.nl)
  • Indeed, this treatment induced changes in the LH2 absorption spectrum related to the disruption of the interaction of B800 molecules with the LH2 protein. (asm.org)
  • Arf and many Arl proteins are modified by addition of a hydrophobic myristoyl group to the amino-terminal amphipathic helix. (frontiersin.org)
  • There are approximately twenty-eight amino acids that combine in various ways to create hundreds of different types of proteins. (shirleys-wellness-cafe.com)
  • Some amino acids enhance the defense system by stimulating the antioxidant activity of certain enzymes and can help prevent skin and coat problems. (shirleys-wellness-cafe.com)
  • Pet foods high in protein may or may not contain all the necessary amino acids to maintain proper health of a pet. (shirleys-wellness-cafe.com)
  • Recombinant protein fragment corresponding to amino acids 97-383 of human AP2M1 (NP_001020376) produced in E.coli. (novusbio.com)
  • The different distribution of fluorescent fusions of the two isoforms was influenced by the nature of an amino acid residue at the C-terminus of the protein, suggesting that the requirements for membrane association of the two GTPases are not equal. (deepdyve.com)
  • The ras protein family: evolutionary tree and role of conserved amino acids. (ebi.ac.uk)
  • Most of these mutations change single protein building blocks (amino acids) in the SEC23B protein. (medlineplus.gov)
  • Active transport mechanisms, primarily in the duodenum and jejunum, absorb most proteins as their breakdown products, amino acids. (amazonaws.com)
  • The coat proteins from the three representative phages, P22, CUS-3, and Sf6, have low amino acid sequence identity (14 to 28%), but all contain a protein domain incorporated within the HK97 fold scaffold, termed the insertion domain (I-domain). (asm.org)
  • The protein encoded by this gene is one of two large chain components of the assembly protein complex 2, which serves to link clathrin to receptors in coated vesicles. (nih.gov)
  • The gene encoding the protein MUDENG (Mu-2 related death-inducing gene) was cloned and characterized. (nih.gov)
  • p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence. (uniprot.org)
  • section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. (uniprot.org)
  • NuA4/Tip60 is a complex which catalyzes diverse substrates critical for gene regulation, DNA repair, and cell cycle progression. (innovations-report.com)
  • OCA2, the product of the gene defective in oculocutaneous albinism type 2, is a melanosomal membrane protein with restricted expression pattern and a potential role in the trafficking of other proteins to melanosomes. (wiley.com)
  • The protein encoded by this gene is a member of the SEC24 subfamily of the SEC23/SEC24 family, which is involved in vesicle trafficking. (genecards.org)
  • AP-3 complex subunit mu-1 is a protein that in humans is encoded by the AP3M1 gene. (wikipedia.org)
  • The SEC23B protein is very similar to the protein produced from a related gene, SEC23A . (medlineplus.gov)
  • Other mutations delete genetic material from the SEC23B gene or alter the way the gene's instructions are used to make the SEC23B protein. (medlineplus.gov)
  • It is an RNA gene-guided editing platform, which is helping to break a double-stranded DNA at a specific location within the genome by making use of a Protein Coat (Cas9) and a synthetic RNA guide. (whitedust.net)
  • Immobilized fibronectin and other natural proteins have been utilized to enhance substrate-mediated gene delivery, with apparent contributions from the intrinsic bioactivity and also physical properties of the immobilized proteins. (pubmedcentralcanada.ca)
  • In this report, we investigated the use of recombinant proteins, compared to the the full-length fibronectin protein, as surface coatings for gene delivery in order to investigate the mechanisms by which fibronectin enhances gene transfer. (pubmedcentralcanada.ca)
  • Recombinant proteins can be employed in place of full-length extracellular matrix proteins for substrate-mediated gene delivery, and bioactive sequences can influence one or more steps in the gene delivery process to maximize transfection. (pubmedcentralcanada.ca)
  • Fibronectin enhances substrate-mediated gene delivery with retroviruses and DNA/polymer complexes, termed polyplexes 14 , 15 . (pubmedcentralcanada.ca)
  • Rogers JV, McMahon C, Baryshnikova A, Hughson FM, Rose MD. ER-associated retrograde SNAREs and the Dsl1 complex mediate an alternative, Sey1p-independent homotypic ER fusion pathway. (harvard.edu)
  • There are three classes of mammalian Arf proteins, Class I (Arfs1-3), Class II (Arfs 4-5), and Class III (Arf6), the division being largely based on sequence homology. (frontiersin.org)
  • There are three classes of mammalian Arf proteins, distinguished by size and homology ( 1 ). (bioscience.org)
  • Approximately one-third of the proteins encoded by the mammalian genome are destined for the secretory pathway. (bloodjournal.org)
  • Examples include: Archain ARFs Clathrin Caveolin Dynamin and related proteins, such as the EHD protein family Rab proteins SNAREs Vesicular transport adaptor proteins e.g. (wikipedia.org)
  • Activated Arfs have several effector proteins. (bioscience.org)
  • Arfs are named for their activity as cofactors for cholera toxin-catalyzed adenosine diphosphate-ribosylation of the heterotrimeric G protein Gs. (sciencemag.org)
  • Protein-protein and protein-metabolite interactions are crucial for all cellular functions. (jove.com)
  • Herein, we describe a protocol that allows parallel analysis of these interactions with a protein of choice. (jove.com)
  • The technique is applied not only to the measurement in real-time of the kinetics of ligand-receptor interactions and to the screening of lead compounds in the pharmaceutical industry, but also to the measurement of DNA hybridization, enzyme-substrate interactions, in polyclonal antibody characterization, epitope mapping, protein conformation studies and label-free immunoassays. (hindawi.com)
  • This simple technology finds application in label-free quantitative immunoassay techniques for proteins and small analytes, in conformational studies with proteins as well as in the real-time association-dissociation measurements of receptor-ligand interactions, for high-throughput screening and lead optimization. (hindawi.com)
  • X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity. (uu.se)
  • The functional organization of eukaryotic cells requires the exchange of proteins, lipids, and polysaccharides between membrane compartments through transport intermediates. (mdpi.com)
  • Until recently, these were not linked, but we have shown that many viruses in this class encode multiple, degenerate RNA sequence/structure motifs that bind cognate coat proteins collectively. (pnas.org)
  • Nevertheless, significant structural differences occur in loops connecting the β-strands, in surface electrostatics used to dock the I-domains with their respective coat protein core partners, and in sequence motifs displayed on the capsid surfaces. (asm.org)
  • Component of the adaptor protein complex 2 (AP-2). (uniprot.org)
  • However, the mechanistic connection between the C-terminal dileucine motif of Nef and the component(s) of the clathrin-coated pits has not been pinpointed. (jimmunol.org)
  • if the proteins work together in complexes, then defects in any one component protein might be expected to compromise function of the complex as a whole. (biologists.org)
  • Molecular evolution of the vesicle coat component betaCOP in Toxoplasma gondii. (biomedsearch.com)
  • It is a component of Coat Protein Complex I . This enzyme was formerly listed as EC 3.6.1.47. (online-medical-dictionary.org)
  • In both of these categories, ABA signaling is not a linear signal-response event, but a complex network involving a number of different signals and effectors. (plantphysiol.org)
  • Several Arf-binding proteins suspected to be effectors have been identified in two-hybrid screens. (sciencemag.org)
  • Despite very low sequence homology, the major capsid proteins of double-stranded DNA (dsDNA) bacteriophages, some archaeal viruses, and the herpesviruses share a structural motif, the HK97 fold. (asm.org)
  • In the "active" state, the GTP-bound GTPases interact with various downstream effector proteins that execute diverse cellular functions. (mdpi.com)
  • Viral proteins recruit and interact with cellular trafficking proteins to divert the normal trafficking of key proteins or to induce the formation of novel membrane structures in the host cell. (bioscience.org)
  • These changes may be a direct result of viral proteins targeting cellular machinery, or an indirect effect associated with viral replication. (bioscience.org)
  • Nef is a crucial viral protein for HIV to replicate at high titers and in the development of AIDS. (jimmunol.org)
  • The cell-to-cell spread of Tobacco mosaic virus infection depends on virus-encoded movement protein (MP), which is believed to form a ribonucleoprotein complex with viral RNA (vRNA) and to participate in the intercellular spread of infectious particles through plasmodesmata. (asm.org)
  • The coat protein (CP) of TMV is dispensable for cell-to-cell movement ( 26 , 96 ), which is consistent with the transport of viral RNA (vRNA) in a nonencapsidated form ( 39 ). (asm.org)
  • Since microinjected MP spreads rapidly between cells ( 77 , 103 ) and plants themselves encode proteins thought to be functionally analogous to viral MPs ( 65 , 108 ), the function of MP may directly reflect mechanisms of macromolecular Pd transport in normal plants which are exploited by viruses for the movement of their genomes. (asm.org)
  • To start the transcription of positive-sense messenger RNA (mRNA) the viral protein must connect with the genomic RNA [ 6 , 7 ]. (intechopen.com)
  • The capsid is self-assembled from viral coat proteins. (asm.org)
  • Viral lineages fall into four families based on the major capsid coat protein structure: PRD1-like, picorna virus-like, HK97-like, and BTV-like ( 1 , 2 ). (asm.org)
  • Today a virus is defined as a minute entity composed of an inner core of nucleic acid contained in a protein envelope. (encyclopedia.com)
  • Although the meaning of "virus" changed considerably from ancient Rome to the early decades of the twentieth century, traces of its original Latin usage can be found in expressions such as "the virus of racism," where it means something that poisons the mind, rather than a minute particle composed of nucleic acid and protein. (encyclopedia.com)
  • Viruses encapsulate their nucleic acids in a protein shell called a capsid that protects the genome until it is delivered to target cells. (asm.org)
  • Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (uniprot.org)
  • The Pvmsp-3 α sequence is remarkably diverse, but this extensive diversity is largely restricted to certain domains of the encoded protein. (cambridge.org)
  • Download DNA or protein sequence, view genomic context and coordinates. (yeastgenome.org)
  • Basic sequence-derived (length, molecular weight, isoelectric point) and experimentally-determined (median abundance, median absolute deviation) protein information. (yeastgenome.org)
  • Click "Protein Details" for further information about the protein such as half-life, abundance, domains, domains shared with other proteins, protein sequence retrieval for various strains, physico-chemical properties, protein modification sites, and external identifiers for the protein. (yeastgenome.org)
  • Sequence comparisons of small G proteins from various species have revealed that they are conserved in primary structures at the level of 30-55% similarity [ PMID: 2029511 ]. (ebi.ac.uk)
  • Membrane protein structures can be determined by X-ray crystallography, electron microscopy or NMR spectroscopy. (wikipedia.org)
  • [7] The most common tertiary structures of these proteins are transmembrane helix bundle and beta barrel . (wikipedia.org)
  • Hence, despite the significant functional importance of membrane proteins, determining atomic resolution structures for these proteins is more difficult than globular proteins. (wikipedia.org)
  • [9] As of January 2013 less than 0.1% of protein structures determined were membrane proteins despite being 20-30% of the total proteome. (wikipedia.org)
  • Possible mechanism for protein particle formation through the interaction between unordered terminal domains and their transformation into β‑structures has been suggested. (springer.com)
  • The results reported here-obtained from a combination of biochemical and biophysical methods-reveal distinct shapes and quaternary structures for each type of complex. (pnas.org)
  • X-ray structures of the maltose-maltodextrin-binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins. (uu.se)
  • IMPORTANCE Comparative studies of protein structures often provide insights into their evolution. (asm.org)
  • Combined immunodeficiency due to a mutation in the ?1 subunit of the coat protein I complex. (childrenshospital.org)
  • Fats, or lipids, have a more complex method of absorption than proteins. (b-naturals.com)
  • In a genomewide screen, the largest class of toxicity modifiers were proteins functioning at this same step, including the Rab guanosine triphosphatase Ypt1p, which associated with cytoplasmic αSyn inclusions. (sciencemag.org)
  • Title: Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration. (nih.gov)
  • Zimmerberg, J. & Kozlov, M. M. How proteins produce cellular membrane curvature. (nature.com)
  • To gain a mechanistic understanding of the various cellular processes, it is crucial to determine the structure of such protein complexes, and reveal how their structural organization dictates their function. (jove.com)
  • The term AP complex, or adaptor, generally denotes one of four heterotetrameric protein complexes (AP-1, AP-2, AP-3, and AP-4) (for reviews, see Refs. (jimmunol.org)
  • The reduction of protein adsorption by a polymer brush formed upon adsorption of Complex Coacervate Core Micelles (C3Ms), consisting of a charged copolymer containing a neutral block and an oppositely charged homopolymer, on silica and polystyrene surfaces has been studied in situ using fixed angle optical reflectometry. (wur.nl)
  • The reduction of protein adsorption by C3Ms was found to be influenced by the surface chemical composition, surface charge, hydrophobicity and salt concentration. (wur.nl)
  • C3M adsorption was higher on hydrophobic polystyrene than on hydrophilic silica, but stronger reduction of protein adsorption was observed on silica. (wur.nl)
  • On the silica surface higher reduction of protein adsorption was observed when micelles carry an excess charge opposite to the charge of the native surface. (wur.nl)
  • Several approaches have been employed for DNA immobilization including DNA entrapment in gelatin 1 , poly-electrolyte layering of DNA 4 , 5 , or immobilization of preformed complexes with specific tethering 3 , 6 , 7 or nonspecific adsorption 2 , 8 - 13 . (pubmedcentralcanada.ca)
  • The support is cheap, easily synthesized, and can be coated with various proteins or protein-ligand complexes by charge adsorption. (hindawi.com)
  • However, the mechanisms coordinating coat assembly, membrane and actin remodelling during post-TGN transport remain poorly understood. (nih.gov)
  • Transport from one compartment of this pathway to another is mediated by vesicular carriers, which are formed by the controlled assembly of coat protein complexes (COPs) on donor organelles. (mdpi.com)
  • Isolated transport vesicles contain membrane and internal proteins that are targeted to other compartments in the cell, but they are nearly devoid of proteins that are located in the ER. (berkeley.edu)
  • Vesicles formed in the transport reaction have an electron-dense, 10-nm coat structure that consists of the Sec proteins (Sar1p, Sec23/24p, and Sec13/31p) required in budding. (berkeley.edu)
  • GTP-binding proteins involved in nucleocytoplasmic transport. (ebi.ac.uk)