Coatomer Protein: 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.Coat Protein Complex I: 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.Golgi Apparatus: 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)Coated Vesicles: 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.COP-Coated Vesicles: 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: 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.ADP-Ribosylation Factors: MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47Saudi Arabia3' Untranslated Regions: The sequence at the 3' end of messenger RNA that does not code for product. This region contains transcription and translation regulating sequences.Nigeria: A republic in western Africa, south of NIGER between BENIN and CAMEROON. Its capital is Abuja.5' Untranslated Regions: The sequence at the 5' end of the messenger RNA that does not code for product. This sequence contains the ribosome binding site and other transcription and translation regulating sequences.Untranslated Regions: The parts of the messenger RNA sequence that do not code for product, i.e. the 5' UNTRANSLATED REGIONS and 3' UNTRANSLATED REGIONS.Molecular Sequence Data: 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.Patents as Topic: Exclusive legal rights or privileges applied to inventions, plants, etc.Toxoplasma: A genus of protozoa parasitic to birds and mammals. T. gondii is one of the most common infectious pathogenic animal parasites of man.HLA-B40 Antigen: A specific HLA-B surface antigen subtype. Members of this subtype contain alpha chains that are encoded by the HLA-B*40 allele family.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Toxoplasmosis: The acquired form of infection by Toxoplasma gondii in animals and man.Amido Black: A dye used to stain proteins in electrophoretic techniques. It is used interchangeably with its acid form.Neurochemistry: The study of the composition, chemical structures, and chemical reactions of the NERVOUS SYSTEM or its components.Ovarian Neoplasms: Tumors or cancer of the OVARY. These neoplasms can be benign or malignant. They are classified according to the tissue of origin, such as the surface EPITHELIUM, the stromal endocrine cells, and the totipotent GERM CELLS.Proteomics: The systematic study of the complete complement of proteins (PROTEOME) of organisms.Adenocarcinoma: A malignant epithelial tumor with a glandular organization.Lysosome-Associated Membrane Glycoproteins: Ubiquitously expressed integral membrane glycoproteins found in the LYSOSOME.Ovary: The reproductive organ (GONADS) in female animals. In vertebrates, the ovary contains two functional parts: the OVARIAN FOLLICLE for the production of female germ cells (OOGENESIS); and the endocrine cells (GRANULOSA CELLS; THECA CELLS; and LUTEAL CELLS) for the production of ESTROGENS and PROGESTERONE.Terminology as Topic: The terms, expressions, designations, or symbols used in a particular science, discipline, or specialized subject area.Databases, Genetic: Databases devoted to knowledge about specific genes and gene products.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Repetitive Sequences, Amino Acid: A sequential pattern of amino acids occurring more than once in the same protein sequence.Shadowing (Histology): The technique of spraying a tissue specimen with a thin coat of a heavy metal such as platinum. The specimen is sprayed from an oblique angle, which results in the uneven deposition of the coating. The varying thicknesses create a shadow effect and give a three-dimensional appearance to the specimen.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.GTP-Binding Proteins: Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.Adenosine Diphosphate Ribose: An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins.Brefeldin A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.RNA Interference: A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.Drosophila: A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.High-Throughput Screening Assays: Rapid methods of measuring the effects of an agent in a biological or chemical assay. The assay usually involves some form of automation or a way to conduct multiple assays at the same time using sample arrays.Drosophila Proteins: Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.Drosophila melanogaster: A species of fruit fly much used in genetics because of the large size of its chromosomes.Genome, Insect: The genetic complement of an insect (INSECTS) as represented in its DNA.Bacterial Proteins: Proteins found in any species of bacterium.rab GTP-Binding Proteins: A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.rab3 GTP-Binding Proteins: A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in calcium-dependent EXOCYTOSIS. This enzyme was formerly listed as EC 3.6.1.47.Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Endoplasmic Reticulum: 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)Serial Publications: Publications in any medium issued in successive parts bearing numerical or chronological designations and intended to be continued indefinitely. (ALA Glossary of Library and Information Science, 1983, p203)Nobel Prizetrans-Golgi Network: A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.Vesicular Transport Proteins: 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.Cell Biology: The study of the structure, behavior, growth, reproduction, and pathology of cells; and the function and chemistry of cellular components.

Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. (1/266)

COPI-coated vesicle budding from lipid bilayers whose composition resembles mammalian Golgi membranes requires coatomer, ARF, GTP, and cytoplasmic tails of putative cargo receptors (p24 family proteins) or membrane cargo proteins (containing the KKXX retrieval signal) emanating from the bilayer surface. Liposome-derived COPI-coated vesicles are similar to their native counterparts with respect to diameter, buoyant density, morphology, and the requirement for an elevated temperature for budding. These results suggest that a bivalent interaction of coatomer with membrane-bound ARF[GTP] and with the cytoplasmic tails of cargo or putative cargo receptors is the molecular basis of COPI coat assembly and provide a simple mechanism to couple uptake of cargo to transport vesicle formation.  (+info)

Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. (2/266)

The crystal structure of the complex of ARF1 GTPase bound to GDP and the catalytic domain of ARF GTPase-activating protein (ARFGAP) has been determined at 1.95 A resolution. The ARFGAP molecule binds to switch 2 and helix alpha3 to orient ARF1 residues for catalysis, but it supplies neither arginine nor other amino acid side chains to the GTPase active site. In the complex, the effector-binding region appears to be unobstructed, suggesting that ARFGAP could stimulate GTP hydrolysis while ARF1 maintains an interaction with its effector, the coatomer complex of COPI-coated vesicles. Biochemical experiments show that coatomer directly participates in the GTPase reaction, accelerating GTP hydrolysis a further 1000-fold in an ARFGAP-dependent manner. Thus, a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats.  (+info)

Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. (3/266)

The Saccharomyces cerevisiae maltose transporter is a 12-transmembrane segment protein that under certain physiological conditions is degraded in the vacuole after internalization by endocytosis. Previous studies showed that endocytosis of this protein is dependent on the actin network, is independent of microtubules, and requires the binding of ubiquitin. In this work, we attempted to determine which coat proteins are involved in this endocytosis. Using mutants defective in the heavy chain of clathrin and in several subunits of the COPI and the COPII complexes, we found that clathrin, as well as two cytosolic subunits of COPII, Sec23p and Sec24p, could be involved in internalization of the yeast maltose transporter. The results also indicate that endocytosis of the maltose transporter and of the alpha-factor receptor could have different requirements.  (+info)

Inhibition of secretion by 1,3-Cyclohexanebis(methylamine), a dibasic compound that interferes with coatomer function. (4/266)

We noted previously that certain aminoglycoside antibiotics inhibit the binding of coatomer to Golgi membranes in vitro. The inhibition is mediated in part by two primary amino groups present at the 1 and 3 positions of the 2-deoxystreptamine moiety of the antibiotics. These two amines appear to mimic the epsilon-amino groups present in the two lysine residues of the KKXX motif that is known to bind coatomer. Here we report the effects of 1, 3-cyclohexanebis(methylamine) (CBM) on secretion in vivo, a compound chosen for study because it contains primary amino groups that resemble those in 2-deoxystreptamine and it should penetrate lipid bilayers more readily than antibiotics. CBM inhibited coatomer binding to Golgi membranes in vitro and in vivo and inhibited secretion by intact cells. Despite depressed binding of coatomer in vivo, the Golgi complex retained its characteristic perinuclear location in the presence of CBM and did not fuse with the endoplasmic reticulum (ER). Transport from the ER to the Golgi was also not blocked by CBM. These data suggest that a full complement of coat protein I (COPI) on membranes is not critical for maintenance of Golgi integrity or for traffic from the ER to the Golgi but is necessary for transport through the Golgi to the plasma membrane.  (+info)

Nef-induced CD4 degradation: a diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes. (5/266)

The Nef protein of primate lentiviruses downregulates the cell surface expression of CD4 through a two-step process. First, Nef connects the cytoplasmic tail of CD4 with adaptor protein complexes (AP), thereby inducing the formation of CD4-specific clathrin-coated pits that rapidly endocytose the viral receptor. Second, Nef targets internalized CD4 molecules for degradation. Here we show that Nef accomplishes this second task by acting as a connector between CD4 and the beta subunit of COPI coatomers in endosomes. A sequence encompassing a critical acidic dipeptide, located nearby but distinct from the AP-binding determinant of HIV-1 Nef, is responsible for beta-COP recruitment and for routing to lysosomes. A novel class of endosomal sorting motif, based on acidic residues, is thus revealed, and beta-COP is identified as its downstream partner.  (+info)

p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway. (6/266)

COPI-coated vesicles that bud off the Golgi complex contain two major transmembrane proteins, p23 and p24. We have localized the protein at the Golgi complex and at COPI-coated vesicles. Transport from the intermediate compartment (IC) to the Golgi can be blocked at 15 degrees C, and under these conditions p24 accumulates in peripheral punctated structures identified as IC. Release from the temperature block leads to a redistribution of p24 to the Golgi, showing that p24, similar to p23, cycles between the IC and Golgi complex. Immunoprecipitations of p24 from cell lysates and from detergent-solubilized Golgi membranes and COPI-coated vesicles show that p24 and p23 interact with each other to form a complex. Transient transfection of p23 in HeLa cells shows that p23 and p24 colocalize in structures induced by the overexpression of p23. Taken together p24 interacts with p23 and constitutively cycles between the organelles of the early secretory pathway.  (+info)

Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COPI dissociation. (7/266)

Physiological conditions that impinge on constitutive traffic and affect organelle structure are not known. We report that osmotically induced cell volume changes, which are known to occur under a variety of conditions, rapidly inhibited endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells. Both ER export and ER Golgi intermediate compartment (ERGIC)-to-Golgi trafficking steps were blocked, but retrograde transport was active, and it mediated ERGIC and Golgi collapse into the ER. Extensive tubulation and relatively rapid Golgi resident redistribution were observed under hypo-osmotic conditions, whereas a slower redistribution of the same markers, without apparent tubulation, was observed under hyperosmotic conditions. The osmotic stress response correlated with the perturbation of COPI function, because both hypo- and hyperosmotic conditions slowed brefeldin A-induced dissociation of betaCOP from Golgi membranes. Remarkably, Golgi residents reemerged after several hours of sustained incubation in hypotonic or hypertonic medium. Reemergence was independent of new protein synthesis but required PKC, an activity known to mediate cell volume recovery. Taken together these results indicate the existence of a coupling between cell volume and constitutive traffic that impacts organelle structure through independent effects on anterograde and retrograde flow and that involves, in part, modulation of COPI function.  (+info)

GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23. (8/266)

A site-directed photocross-linking approach was employed to determine components that act downstream of ADP-ribosylation factor (ARF). To this end, a photolabile phenylalanine analog was incorporated at various positions of the putative effector region of the ARF molecule. Depending on the position of incorporation, we find specific and GTP-dependent interactions of ARF with two subunits of the coatomer complex, beta-COP and gamma-COP, as well as an interaction with a cytosolic protein (approximately 185 kDa). In addition, we observe homodimer formation of ARF molecules at the Golgi membrane. These data suggest that the binding site of ARF to coatomer is at the interface of its beta- and gamma-subunits, and this is in close proximity to the second site of interaction of coatomer with the Golgi membrane, the binding site within gamma-COP for cytosolic dibasic/diphenylalanine motifs.  (+info)

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).
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.
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 ...
Among all retroviruses, foamy viruses (FVs) are unique in that they regularly mature at intracytoplasmic membranes. The envelope glycoprotein of FV encodes an endoplasmic reticulum (ER) retrieval signal, the dilysine motif (KKXX), that functions to localize the human FV (HFV) glycoprotein to the ER. This study analyzed the function of the dilysine motif in the context of infectious molecular clones of HFV that encoded mutations in the dilysine motif. Electron microscopy (EM) demonstrated virion budding both intracytoplasmically and at the plasma membrane for the wild-type and mutant viruses. Additionally, mutant viruses retained their infectivity, but viruses lacking the dilysine signal budded at the plasma membrane to a greater extent than did wild-type viruses. Interestingly, this relative increase in budding across the plasma membrane did not increase the overall release of viral particles into cell culture media as measured by protein levels in vital pellets or infectious virus titers. We ...
plant Sar1 (ER marker) , Q8VYP7, AS08 326, Sar1 belongs to a small GTPase superfamily and GTP binging activity. This protein is involved in intracellular protein transport. There are two different non-clathrin-coated vesicle
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.
The gene that encodes ARCN1 maps in a region, which includes the mixed lineage leukemia and Friend leukemia virus integration 1 genes, where multiple…
Characterisation of a delta-COP homologue in the malaria parasite, Plasmodium falciparum.: The mature human erythrocyte is a simple haemoglobin-containing cell
Coatomer subunit gamma ; 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 (899 aa ...
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 ...
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 ...
Membrane, Proteins, Endoplasmic Reticulum, Reticulum, Secretory Pathway, Yeast, Gtpase, Coated Vesicles, Copi, Copi-coated Vesicles, and Clathrin
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
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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ウサギ・ポリクローナル抗体 ab2913 交差種: Rat,Hu,NHuPrm 適用: WB,IP,ICC…alpha COP I抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。
DRTS_LEIAM (P16126 ), DRTS_LEIMA (P07382 ), DRTS_MAIZE (O81395 ), DRTS_ORYSJ (Q2QRX6 ), DRTS_PARTE (Q27828 ), DRTS_PLABA (Q27713 ), DRTS_PLACH (P20712 ), DRTS_PLAFK (P13922 ), DRTS_PLAVI (O02604 ), DRTS_PLAVN (P46103 ), DRTS_SOYBN (P51820 ), DRTS_TOXGO (Q07422 ), DRTS_TRYBB (Q27783 ), DRTS_TRYCR (Q27793 ), DYR10_ECOLX (Q04515 ), DYR13_ECOLX (Q59408 ), DYR15_ECOLX (P78218 ), DYR1_ECOLX (P00382 ), DYR1_HALMA (Q5V3R2 ), DYR2_HALMA (Q5V600 ), DYR3_SALTM (P12833 ), DYR5_ECOLX (P11731 ), DYR6_PROMI (P95524 ), DYR7_ECOLX (P27422 ), DYR8_ECOLX (P0ABQ7 ), DYR8_SHISO (P0ABQ8 ), DYR9_ECOLX (Q59397 ), DYRA_HALVD (P15093 ), DYRA_STAAU (P13955 ), DYRB_HALVO (Q9UWQ4 ), DYR_AEDAL (P28019 ), DYR_BACSU (P11045 ), DYR_BOVIN (P00376 ), DYR_BPT4 (P04382 ), DYR_BUCAI (P57243 ), DYR_BUCAP (Q8K9Z8 ), DYR_BUCBP (Q89AV2 ), DYR_CAEEL (Q93341 ), DYR_CANAX (P22906 ), DYR_CHICK (P00378 ), DYR_CITFR (P31073 ), DYR_CRYNJ (Q07801 ), DYR_DROME (P17719 ), DYR_ECOL6 (P0ABQ5 ), DYR_ECOLI (P0ABQ4 ), DYR_ENTFC (P00380 ), DYR_HAEIN ...
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
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
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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., ...
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 ...
gi,17538522,ref,NP_501092.1, component of oligomeric Golgi complex 2; brefeldin A-sensitive, LDLC related peripheral Golgi protein, required for normal Golgi function; contains an N myristoylation domain (78.6 kD) (4H802) [Caenorhabditis elegans] gi,2498513,sp,Q21444,COG2_CAEEL Conserved oligomeric Golgi complex component 2 (LDLC protein homolog) gi,1078836,pir,,B53542 brefeldin A-sensitive Golgi protein LDLC - Caenorhabditis elegans gi,807871,emb,CAA84428.1, Cog2 protein [Caenorhabditis elegans] ...
The nucleotide sequences of the nucleoprotein (NP) genes of fowl plague virus (FPV) and of a temperature-sensitive (ts) mutant (ts81) derived therefrom have been determined. The ts81-NP nucleotide sequence possesses a single nucleotide substitution in comparison to the wild type. This causes an amin …
COPⅠ囊泡:最初研究者利用三磷酸鳥苷(GTP)衍生物GTPγS(一種富含高爾基體膜的細胞質與抗水解的GTP衍生物)共培養時,發現高爾基體池之間存在一種囊泡轉運結構[9](後來在真核細胞中也證實此結構的存在[10])。除了脂質成分外,參與此囊泡形成的成份還有7種外被體蛋白(即外被體α、β、β′、γ、δ、ε、ζ)。這些外被體蛋白相互作用形成的復合物就是COPⅠ囊泡[11][12]。亞單位α、β′、ε在結構上與網格蛋白及COPⅡ囊泡的外層組分具有較高的一致性,形成復合物的內層組分稱為B亞復合物(主要負責與靶蛋白結合),而亞單位β、γ、δ、ζ 與網格蛋白及COPⅡ囊泡的內層組分相似,形成復合物的內層組分稱為F亞復合物,該亞復合物主要負責與靶蛋白結合,並且直接與COPⅠ囊泡形成的招募者ADP核糖基化因子(英语:ADP ribosylation factor)(ADP ribosylation ...
1FQE: Crystal structures and iron release properties of mutants (K206A and K296A) that abolish the dilysine interaction in the N-lobe of human transferrin.
Endogenous hHK3 localizes to the Golgi complex. The localization of endogenous Hook proteins in Hep2 cells (A, D, G, J, and M) was compared with the Golgi marke
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TY - JOUR. T1 - ADP ribosylation factor 6 regulates neuronal migration in the developing cerebral cortex through FIP3/arfophilin-1-dependent endosomal trafficking of N-cadherin. AU - Hara, Yoshinobu. AU - Fukaya, Masahiro. AU - Hayashi, Kanehiro. AU - Kawauchi, Takeshi. AU - Nakajima, Kazunori. AU - Sakagami, Hiroyuki. PY - 2016. Y1 - 2016. N2 - During neural development, endosomal trafficking controls cell shape and motility through the polarized transport of membrane proteins related to cellcell and cellextracellular matrix interactions. ADP ribosylation factor 6 (Arf6) is a critical small GTPase that regulates membrane trafficking between the plasma membrane and endosomes. We herein demonstrated that the knockdown of endogenous Arf6 in mouse cerebral cortices led to impaired neuronal migration in the intermediate zone and cytoplasmic retention of N-cadherin and syntaxin12 in migrating neurons. Rescue experiments with separation-of-function Arf6 mutants identified Rab11 familyinteracting ...
View Notes - Lecture 13 11 from BICD 110 at UCSD. Lecture 13 11/02/07 Golgi Structure/Function, Lysosome, Exocytosis Glycosylation Protects lysosome membrane proteins from autodegradation
The mammalian Golgi complex is composed of stacks of flattened cisternae linked through tubules to form a contiguous juxtanuclear ribbon. The stacked cisternae reflect the compartmentalization of Golgi enzymes for the processing of transiting cargo (Mellman and Simons, 1992; Puthenveedu and Linstedt, 2005). Cargo movement through the stack has been variously suggested to occur in vesicles, in maturing cisternae, or by tubular connections between cisternae (Malhotra et al., 1989; Mollenhauer and Morre, 1991; Glick et al., 1997; Allan and Balch, 1999; Pelham and Rothman, 2000; Trucco et al., 2004). Although not exclusive of other processes, maturation has gained recent support (Emr et al., 2009). This model starts with the creation of cargo-containing cis-Golgi cisternae. The cargo stays within these cisternae and is sequentially processed when the cis enzymes are replaced with medial enzymes, which are subsequently replaced with trans enzymes. As cisternae progress through the Golgi stack, this ...
We do a complete analysis and explanation behind Hakkers stacks and routines. He had the MENS stack, HUSS routine, Hybrid Stack, and the H4GS routine stack.
Regarding the biogenesis of peroxisomes various concepts have been postulated. Based on morphological data that demonstrated close spatial relationships between peroxisomes and the ER, Novikoff and Novikoff (44) favored the idea that new peroxisomes are formed by budding and fission from the ER. However, a series of biochemical studies initiated by de Duve and coworkers (36, 51) in the early 1970s, focusing on the biogenetic route of catalase as a peroxisomal marker, did not reveal an ER involvement in the import of catalase. Subsequent findings of Goldman and Blobel (19) and particularly the group of Lazarow and coworkers (52, 54) confirmed this view demonstrating that peroxisomal matrix proteins, such as catalase, urate oxidase, and enzymes of the peroxisomal β-oxidation pathway, are synthesized on free polyribosomes and thus are imported posttranslationally. Accordingly, Goldman and Blobel (19) postulated a model in which peroxisomal matrix proteins are found in nascent peroxisomes, whereas ...
Transition zones are associated with the Golgi stacks. They are close to each other. This makes sense because the communication is more efficient. Vesicles dont need to travel long distances and the existence of the Golgi apparatus itself depends on a continuous process of vesicle incoming. It has been observed that a new transition zone led quickly to the nearby formation of a new Golgi stack. On the contrary, if a transition zone disappears, the associated Golgi cisternae are also lost. Transition zones can fuse with others and one transition zone can be split in two. Their associated Golgi stacks match this behavior. Vesicles budding from the transition zones are COPII coated vesicles ( COPII: coat protein II; Figure 1). Several proteins are involved in the formation of this COPII molecular framework: Sec16, Sar1 GTPases, Sec23/24 and Sec13/31. In this order, they are assembled at the cytosolic surface of the transition zone membranes. Transition zones are the more suitable environments for ...
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 ...
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.
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Complete information for ARF6 gene (Protein Coding), ADP Ribosylation Factor 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is involved in the maintenance of Golgi structure and function through its interaction with the integral membrane protein giantin. It may also be involved in the hormonal regulation of steroid formation. [provided by RefSeq, Jul 2008 ...
Complete information for ARL6IP6 gene (Protein Coding), ADP Ribosylation Factor Like GTPase 6 Interacting Protein 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
The Golgi apparatus is a packaging center Golgi apparatus or Golgi body or Golgi complex is a membrane-bound organelle, associated with the processing of…
Fluorescent and time lapse microscopy, advantages of multiplex analysis and the Golgi apparatus. Please donwload this free white paper for more inform
A golgi apparatus, or golgi complex, is the main organelle responsible for mediating the transportation of protein and fat within the cell, according to Scitable, a learning website curated by...
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Lcdproc] [PATCH] FreeBSDs new USB stack support (configure.in changes, testing needed), Andre Guibert de Bruet, 01/26/2009 ...
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 ...
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: ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Arsenic atom in PDB 1r4x: Crystal Structure Analys of the Gamma-Copi Appendage Domain
Giantin (10 nm gold) and rBet1 (15 nm gold) show different distribution patterns. Most of the cells giantin is present in the Golgi complex (G) and associated
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The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds ... "Entrez Gene: COPE coatomer protein complex, subunit epsilon". Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene. ...
Coatomer subunit gamma is a protein that in humans is encoded by the COPG gene. It is one of seven proteins in the COPI ... "Entrez Gene: COPG coatomer protein complex, subunit gamma". Bermak, Jason C; Li Ming; Bullock Clayton; Weingarten Paul; Zhou ... 2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi: ... "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell Biol. ...
Coatomer subunit alpha is a protein that in humans is encoded by the COPA gene. In eukaryotic cells, protein transport between ... "Entrez Gene: COPA coatomer protein complex, subunit alpha". Gerich B, Orci L, Tschochner H, Lottspeich F, Ravazzola M, Amherdt ... 1997). "Association of coatomer proteins with the beta-receptor for platelet-derived growth factor". Biochem. Biophys. Res. ... 1996). "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell ...
Coatomer subunit gamma-2 is a protein that in humans is encoded by the COPG2 gene. COPG2 has been shown to interact with ... "Entrez Gene: COPG2 coatomer protein complex, subunit gamma 2". Bermak JC, Li M, Bullock C, Weingarten P, Zhou QY (Feb 2002). " ... Waters MG, Serafini T, Rothman JE (1991). "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/ ...
Coatomer subunit zeta-1 is a protein that in humans is encoded by the COPZ1 gene. COPZ1 has been shown to interact with COPG. ... COPZ1 coatomer protein complex, subunit zeta 1". Futatsumori M, Kasai K, Takatsu H, Shin HW, Nakayama K (November 2000). " ... "Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complex". J. Cell Biol. ... Pavel J, Harter C, Wieland FT (1998). "Reversible dissociation of coatomer: functional characterization of a beta/delta-coat ...
"The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase Cepsilon". J. Biol. Chem. 272 (46): 29200 ... Coatomer subunit beta' is a protein that in humans is encoded by the COPB2 gene. The Golgi coatomer complex (see MIM 601924) ... "Entrez Gene: COPB2 coatomer protein complex, subunit beta 2 (beta prime)". Eugster A, Frigerio G, Dale M, Duden R (August 2000 ... "Assignment of the cellular retinol-binding protein 1 gene (RBP1) and of the coatomer beta subunit gene (COPB2) to human ...
Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene. GRCh38: Ensembl release 89: ENSG00000129083 - ... 1997). "Association of coatomer proteins with the beta-receptor for platelet-derived growth factor". Biochem. Biophys. Res. ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Pavel J, Harter C, Wieland FT (1998). "Reversible dissociation of coatomer: Functional characterization of a β/δ-coat protein ...
Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles.. Nature. 1991-01-17 ... 運輸囊泡(Transport vesicles)在真核生物中,通過在不同細胞器及細胞表面進行轉運發揮它的作用。目前已知的運輸囊泡有網格蛋白囊泡、外被體蛋白(英语:Coat protein)Ⅰ(coat protein、COPI(英语:COPI)囊泡)和 ... Lee, C; Goldberg, J. Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle
... is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to ... 1994). "Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum". Cell. 79 (7): 1199-207. ... 1. Luminal proteins: Proteins found in the lumen of the Golgi complex that need to be transported to the lumen of the ER ... 1996). "A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding". J Cell Biol. 135 (5 ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... 2000). "A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. doi:10.1038 ... The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... The gene products include 5 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ... ADP-ribosylation factor 4 is a protein that in humans is encoded by the ARF4 gene. ADP-ribosylation factor 4 (ARF4) is a member ... Shin OH, Ross AH, Mihai I, Exton JH (1999). "Identification of arfophilin, a target protein for GTP-bound class II ADP- ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (1999). "Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a ... Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA (October 1999). "Arf proteins bind to mitotic kinesin-like protein 1 ( ... The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF ...
Waters MG, Serafini T, Rothman JE (1991). "'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. PMID ... "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. PMC 1847948. PMID ... Koatomerna podjedinica gama-2 je protein koji je kod ljudi kodiran COPG2 genom.[1][2][3] ...
These vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction ... AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ...
... is a coatomer, a type of vesicle coat protein that transports proteins from the rough endoplasmic reticulum to the Golgi ... The coat consists of large protein subcomplexes that are made of four different protein subunits. There are two protein ... These proteins are Sec23p/Sec24p Heterodimer Sec13p/Sec31p Heterotetramer These proteins alone are not able to cause the ... SNARE, cargo, and other proteins are also needed for these processes to occur. The CopII protein does, however, cause the ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... ARF6 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH) Human ARF6 genome location and ARF6 ... D'Souza-Schorey C, Boshans RL, McDonough M, Stahl PD, Van Aelst L (1997). "A role for POR1, a Rac1-interacting protein, in ARF6 ... ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety ...
They are also common in membrane coat proteins known as coatomers, such as clathrin, and in regulatory proteins that form ... The protein-protein interaction capacity of alpha solenoid proteins also makes them well suited to function as regulatory ... extended protein-protein interaction surfaces or to form deep concave areas for binding globular proteins. Because they are ... "When protein folding is simplified to protein coiling: the continuum of solenoid protein structures". Trends in Biochemical ...
Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between ... Adaptor protein (AP) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to ... Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. These ...
Components of COPI (cop one) a coatomer, and TSET (T-set) a membrane trafficking complex have similar heterotetramers of the AP ... In the AP complexes, there are two large proteins (∼100 kD) and two smaller proteins. One of the large proteins is termed β ( ... PTBs are protein domains that include NUMB, DAB1 and DAB2. Epsin and AP180 in the ANTH domain are other adaptor proteins that ... The individual proteins of the COPII complex are called SEC proteins, because they are encoded by genes identified in secretory ...
1999). "Assignment of the cellular retinol-binding protein 1 gene (RBP1) and of the coatomer beta subunit gene (COPB2) to human ... Retinol binding protein 1, cellular, also known as RBP1, is a protein that in humans is encoded by the RBP1 gene. RBP1 is the ... "The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane ... Alteration of relative protein amounts is linked to the state of differentiation". Biochem. J. 287. ( Pt 2): 383-9. PMC 1133176 ...
The coatomer is a protein complex that coats membrane-bound transport transport vesicles. Two types of coatomers are known: ... Coatomer Protein at the US National Library of Medicine Medical Subject Headings (MeSH) Boehm, Markus; Bonifacino, Juan S. ( ... Coatomers are functionally analogous and evolutionarily homologous to clathrin adaptor proteins, also known as adaptins, which ...
2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. ... Scyl1 localizes to the cis-Golgi and ER-Golgi Intermediate Compartment (ERGIC). Scyl1 binds to Coatomer I (COPI) and ... This gene encodes a transcriptional regulator belonging to the SCY1-like family of kinase-like proteins. The protein has a ... The FL protein contains HEAT repeats and a C-terminal coiled coil domain that also contains multiple dibasic motifs, and ends ...
... is a protein located on chromosome 11. Also known as ARCH1, it plays a role in eukaryotic cell biology. It is part of ... the COPI coatomer complex. Xu X, Kedlaya R, Higuchi H, et al. (2010). "Mutation in archain 1, a subunit of COPI coatomer ...
2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs ... 2004). "The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex". J. Biol. Chem. 278 (52): 52689- ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (6): 355-64. doi: ... The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (6): 347-55. doi: ...
... including 6 ARF proteins and 11 ARF-like proteins, constitute a family of the RAS superfamily. The ARF proteins are categorized ... Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions ... The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively ... ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene. ADP-ribosylation factor 1 (ARF1) is a member ...
Two examples of adaptor proteins are AP180[3] and epsin.[4][5][6] AP180 is used in synaptic vesicle formation. It recruits ... Clathrin is a protein that plays a major role in the formation of coated vesicles. Clathrin was first isolated and named by ... Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. The endocytosis ... In a cell, a triskelion floating in the cytoplasm binds to an adaptor protein, linking one of its feet to the membrane at a ...
... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be ... which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex ... The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- ... recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also ...
... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be ... which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex ... The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- ... role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. ...
... which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex ... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). ... The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- ... IPR016391. Coatomer_asu. IPR010714. Coatomer_asu_C. IPR006692. Coatomer_WD-assoc_reg. IPR020472. G-protein_beta_WD-40_rep. ...
... functionality is dependent on coatomer protein I (COPI). Together they form a unique fingerprint. * Coatomer Protein Medicine ... In the present study, we identified a role for the COPI (coatomer protein I) cellular trafficking machinery in the development ... In the present study, we identified a role for the COPI (coatomer protein I) cellular trafficking machinery in the development ... In the present study, we identified a role for the COPI (coatomer protein I) cellular trafficking machinery in the development ...
Coatomer-dependent protein delivery to lipid droplets.. Soni KG, Mardones GA, Sougrat R, Smirnova E, Jackson CL, Bonifacino JS. ... Imaging intracellular fluorescent proteins at nanometer resolution.. Betzig E, Patterson GH, Sougrat R, Lindwasser OW, Olenych ... Human immunodeficiency virus type 1 Nef protein targets CD4 to the multivesicular body pathway. ...
Coatomer protein complex, subunit epsilon. COPE. 263. 1179. NM_001861. Cytochrome c oxidase subunit IV isoform 1. COX4I1. 129. ... Preferred therapeutic proteins are interferones, growth factors, anti-angiogenesis proteins, apoptosis modulating proteins, ... The proteins can be either expressed in a secreted form or in cellular compartments. The expressed proteins can further be ... When proteins are expressed transiently a foreign gene that codes for the particular protein is expressed by recipient/host ...
Our focus is on betaCOP, one of the most well known components of the COPI multi-protein complex. Amino acid differences in be ... Coatomer coated (COPI) vesicles play a pivotal role for multiple membrane trafficking steps throughout the eukaryotic cell. ... 0/Coatomer Protein; 0/DNA Primers; 0/DNA, Protozoan; 0/Protozoan Proteins ... Coatomer Protein / genetics*. DNA Primers / genetics. DNA, Protozoan / genetics. Evolution, Molecular. Genes, Protozoan. Models ...
coatomer protein complex, subunit epsilon. MGI:1891702 1 matching records from 1 references.. Summary by Age and Assay: Numbers ...
Coatomer protein complex, subunit beta 1. 1.85. 1.52. N/A. 21070976. Diablo homolog. N/A. 1.54. 1.50. ... 10 μg total protein lysates loaded. Protein levels were normalized to actin loading control. Aconitase 2 is detected at ∼80 kDa ... Table I Significantly changed proteins post-EGF exposure; proteins identified with significant changes following EGF treatment ... subcellular distribution of all proteins significantly altered following EGF treatment (n = 294 proteins across 48 h time ...
Abbreviation for coatomer protein.. COP. 1. Capillary osmotic pressure.. 2. Colloid oncotic pressure. ...
In this review, we will summarize recent advances in regard to LD-related membrane trafficking proteins and discuss future ... In this review, we will summarize recent advances in regard to LD-related membrane trafficking proteins and discuss future ... In recent years, multiple membrane trafficking proteins have been identified through LD proteomics and genetic analyses. These ... In recent years, multiple membrane trafficking proteins have been identified through LD proteomics and genetic analyses. These ...
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- ... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be ... PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Lysates. Multiplex miRNA assays. By ...
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- ... and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Lysates. Multiplex Assays. By ... The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating ...
coatomer subunit zeta-1 [Source:RefSeq peptide;Acc:NP_571583]. Human Orthologue:. COPZ1. Human Description:. coatomer protein ... coatomer protein complex, subunit zeta 1 Gene [Source:MGI Symbol;Acc:MGI:1929063]. ...
coatomer protein complex, subunit beta 1 [Source:HGNC Symbol;Acc:2231]. Mouse Orthologue:. Copb1. Mouse Description:. coatomer ... coatomer subunit beta [Source:RefSeq peptide;Acc:NP_001002013]. Human Orthologue:. COPB1. Human Description:. ... protein complex, subunit beta 1 Gene [Source:MGI Symbol;Acc:MGI:1917599]. ...
Abbreviation for coatomer protein.. COP. 1. Capillary osmotic pressure.. 2. Colloid oncotic pressure. ...
coatomer protein complex subunit alpha. HEP-COP. 1q23.2. COPB2 coatomer protein complex subunit beta 2. beta-COP, betaprime- ... syntaxin binding protein 5 like. KIAA1006, LLGL4. 3q13.33. TAF5 TATA-box binding protein associated factor 5. TAF2D. TAFII100. ... POC1 centriolar protein B. WDR51B. TUWD12, FLJ14923. 12q21.33. PPP2R2A protein phosphatase 2 regulatory subunit Balpha. PR52A, ... mitogen-activated protein kinase binding protein 1. KIAA0596. 15q15.1. MED16 mediator complex subunit 16. THRAP5. DRIP92, ...
coatomer protein complex, subunit alpha. 5285498. Incomplete. BC037941. coatomer protein complex, subunit alpha. ... Protein Similarities Based on Shared Motif Content. Find gene products sharing protein motifs with: NP_004362 Protein ... BP] intracellular protein transport *[BP] pancreatic juice secretion *[BP] retrograde vesicle-mediated transport, Golgi to ER * ...
coatomer protein complex, subunit beta 1. Protein Similarities Based on Shared Motif Content. ... BP] intracellular protein transport *[BP] protein transport *[BP] transport *[BP] vesicle-mediated transport *[CC] COPI vesicle ...
The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds ... "Entrez Gene: COPE coatomer protein complex, subunit epsilon". Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Coatomer subunit epsilon is a protein that in humans is encoded by the COPE gene. ...
Coatomer: a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles.. Nature. 1991-01-17 ... 運輸囊泡(Transport vesicles)在真核生物中,通過在不同細胞器及細胞表面進行轉運發揮它的作用。目前已知的運輸囊泡有網格蛋白囊泡、外被體蛋白(英语:Coat protein)Ⅰ(coat protein、COPI(英语:COPI)囊泡)和 ... Lee, C; Goldberg, J. Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle
May mediate binding of coatomer proteins to the peroxisomal membrane (By similarity). Promotes membrane protrusion and ... Protein-protein interaction databases. STRING: functional protein association networks. More...STRINGi. 10090. ... to allow unambiguous identification of a protein.,p>,a href=/help/protein_names target=_top>More...,/a>,/p>Protein namesi. ... section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes ...
Seven coat proteins have been identified and they represent subunits of a complex known as coatomer. The subunits are ... In eukaryotic cells protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non- ... The alpha-COP encoded by COPA shares high sequence similarity with RET1P the alpha subunit of the coatomer complex in yeast. ...
... β-coatomer protein) (orange), and DIAP (red). βCOP is required for general secretion and viability and DIAP (Drosophila ... E, Protein sequence homology between Drosophila Paf-AHα and human PAFAH1B2 demonstrates a highly conserved protein. Green boxes ... 2A). The protein levels of APP and actin were unaffected. Likewise, the level of NCT and the maturation of this protein, a key ... Aβ is derived from amyloid precursor protein (APP), a type I transmembrane protein that traffics through the secretory pathway ...
Coatomer Protein. *Cricetinae. *Cytoplasm/metabolism. *Fluorescent Antibody Technique, Indirect. *Microtubule-Associated ... p53/58 is a transmembrane protein that continuously recycles between the ER and pre-Golgi intermediates composed of vesicular- ... p53/58 is a transmembrane protein that continuously recycles between the ER and pre-Golgi intermediates composed of vesicular- ... required for the coupled exchange of COPII for COPI coats during segregation of anterograde and retrograde transported proteins ...
  • GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). (uniprot.org)
  • Arf1 is the founding member of the family, and was originally identified as a protein factor required for the ADP-ribosylation of the adenylate cyclase activator Gsα by cholera toxin ( Kahn and Gilman, 1986 ). (biologists.org)
  • Although previously speculated, our results now demonstrate a function for coatomer in ArfGAP-catalyzed GTP hydrolysis by Arf1. (rupress.org)
  • A 100-1,000-fold stimulatory effect of coatomer on GTP hydrolysis was described for the catalytical domain of ArfGAP1 when a soluble version of Arf1, NΔ17Arf1, was used ( Goldberg, 1999 ). (rupress.org)
  • 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)
  • This study shows that coatomer couples sorting signal recognition to the GTP hydrolysis reaction on ARF1. (nih.gov)
  • The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6). (wikipedia.org)
  • They are recruited to the membrane by the small G proteins Arf1 and Sar1, respectively, which in turn are converted into their active GTP-bound states by membrane-associated nucleotide-exchange factors. (rupress.org)
  • Rapid membrane binding and dissociation of coatomer and Arf1 occur stochastically, even without vesicle budding. (nih.gov)
  • This role for Arf1/coatomer might provide a model for investigating the behaviour of other coat protein systems within cells. (nih.gov)
  • An almost universal feature of coat assembly is the recruitment of the various adaptor complexes to the "donor" membrane by the protein Arf1. (wikipedia.org)
  • Budding is mediated by coats, which are cytosolic proteins that bind to a membrane, induce curvature, and eventually pinch off a vesicle (for review see Schekman and Orci, 1996 ). (rupress.org)
  • but also to play a role in quality control, since Kar2p retention in the ER depends on p24 proteins ( Elrod-Erickson and Kaiser, 1996 ), and since knock-out of some family members triggers the unfolded protein response ( Belden and Barlowe, 2001 ). (biologists.org)
  • Molecular chaperones bind nonnative protein conformations, sequestering misfolded protein or aggregation-prone folding intermediates from the cytosol, thereby reducing the likelihood of aggregate formation ( Hartl, 1996 ). (rupress.org)
  • Retrograde transport along the exocytic pathway is the flux of proteins and lipids from later to earlier exocytic compartments, reversing the order of organelle entry with respect to the anterograde transport. (rupress.org)
  • Because they can be purified and added exogenously to cells, retrograde transport of toxin proteins is initially unidirectional, in contrast to the recycling behavior of ER residents, KDEL-receptor (KDELR), or p24 proteins, thus allowing observation of retrograde transport in the absence of concurrent anterograde transport. (rupress.org)
  • This type of transport is termed as retrograde transport, in contrast to the anterograde transport associated with the COPII protein. (wikipedia.org)
  • Luminal ER proteins may be retrieved by means of a C‐terminal KDEL sequence that binds to the KDEL receptor to trigger retrograde transport ( Lewis and Pelham, 1992 ). (embopress.org)
  • Tight spatial and temporal regulation of the relatively small number of Arf proteins is achieved by their guanine nucleotide-exchange factors (GEFs) and GTPase-activating proteins (GAPs), which catalyze GTP binding and hydrolysis, respectively. (biologists.org)
  • The interconversion between GTP and GDP bound states is mediated by ARF guanine nucleotide exchange factors (GEFs) and ARF GTPase activating proteins (GAPs). (wikipedia.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)
  • 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)
  • By contrast, the dilysine retrieval signal, which competes for the same binding site on coatomer, has no effect on GTPase activity. (nih.gov)
  • Mutations of the SM protein Sly1 resulting in bypass of GTPase requirement in vesicular transport are confined to a short helical region. (mpg.de)
  • The GTPase Sar1p is a protein that hydrolyzes GTP and acts like a molecular "switch" that flips between an activated and membrane embedded GTP-bound form, and inactive and soluble GDP-bound form. (wikipedia.org)
  • RGS2 functions as a GTPase Activating Protein (GAP) which acts to increase the natural GTPase activity of the Gα subunit. (wikipedia.org)
  • Whether and how cargo proteins are recruited upstream of Sar1 and COPII is unclear. (biologists.org)
  • The primary function of adaptors is the selection of cargo proteins for their incorporation into nascent carriers. (wikipedia.org)
  • With nonidentical compartments established in this way, the localization and cellular transport of cargo proteins can be explained simply by their affinity for coats. (rupress.org)
  • In this Topical Review, we present their main protein components and discuss current models for cargo sorting. (deepdyve.com)
  • The sorting and concentration of cargo proteins within ER exit sites (ERESs) is a fundamental function of the secretory machinery. (biologists.org)
  • The dynamics of the ER to ERES redistribution of cargo proteins was quantified in single cells by measuring changes in fluorescence-intensity variance after shift to the permissive temperature. (biologists.org)
  • Sar1, in its membrane-associated, GTP-bound form, sequentially recruits cargo proteins and the heterodimers Sec23/24 and Sec13/31. (biologists.org)
  • This dynamic outer shell of the COPII coat complex has been shown to interact with targeting signals of cargo proteins ( Votsmeier and Gallwitz, 2001 ), as well as to affect various features of the membrane, such as curvature and possibly lipid composition ( Graham, 2004 ). (biologists.org)
  • Thus, the actual sorting and concentration of cargo proteins in ERESs is presumed to be driven by more than one type of interaction. (biologists.org)
  • AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. (uniprot.org)
  • SNARE, cargo, and other proteins are also needed for these processes to occur. (wikipedia.org)
  • Due to their propensity for forming large interaction surfaces well-suited to protein-protein interactions, and their flexible surfaces permitting binding of various cargo molecules, alpha solenoid proteins commonly function as transport proteins, particularly in transport between the nucleus and the cytoplasm. (wikipedia.org)
  • The functional organization of eukaryotic cells requires the exchange of proteins, lipids, and polysaccharides between membrane compartments through transport intermediates. (mdpi.com)
  • The bidirectional traffic would tend to equalize the composition of the compartments, yet most proteins and some lipids are concentrated in one organelle and define its identity. (rupress.org)
  • The secretory pathway is comprised of membrane-bound organelles, each defined by a unique composition of proteins and lipids that serve a distinct set of functions. (biologists.org)
  • When human proteins are mapped to yeast, we find a strong positive correlation (r = 0.50, P = 3.9 × 10 -4 ) between evolutionary conservation and the number of interacting proteins, which is also found when mapped to other model organisms. (biomedcentral.com)
  • Human proteins, like yeast proteins, show a correlation between the number of interacting partners and evolutionary conservation. (biomedcentral.com)
  • A combination of low-throughput (LTP) and HTP interaction studies have produced large networks of interacting proteins in Homo sapiens (human), Rattus norvegicus (rat), Mus musculus (mouse), Drosophila melanogaster (fly), Caenorhabditis elegans (worm), and Saccharomyces cerevisiae (yeast) (see Additional data file 1 for sources). (biomedcentral.com)
  • In the past 15 years, studies of yeast ( Saccharomyces cerevisiae ) and metazoan cells have revealed a common core of protein factors involved in transport carrier formation, compartment specificity and membrane fusion ( Bonifacino and Glick, 2004 ). (biologists.org)
  • Yeast and mammalian ER retention motifs interacted specifically in cell lysates with the coatomer, a polypeptide complex implicated in membrane traffic. (sciencemag.org)
  • These results suggest a role for the coatomer in the retrieval of transmembrane proteins to the ER in both yeast and mammals. (sciencemag.org)
  • Abgent has over fifteen years of experience producing recombinant proteins in E. coli and mammalian cells (CHO and HEK293, etc), and we have added a powerful yeast expression platform to our menu of services. (abgent.com)
  • Use1p is a yeast SNARE protein required for retrograde traffic to the ER. (mpg.de)
  • The transport protein particle ( TRAPP ) was initially identified as a vesicle tethering factor in yeast and as a guanine nucleotide exchange factor ( GEF ) for Ypt1/Rab1. (embopress.org)
  • Schekman R (1985) Protein localization and membrane traffic in yeast. (springer.com)
  • These PEX genes code for proteins, called peroxins, which are involved in peroxisome assembly and maintenance ( 5 ). (mcponline.org)
  • includes protein coordinates for the domain, a domain Description, a Source and corresponding accession ID, and the number of S. cerevisiae genes that share the same domain. (yeastgenome.org)
  • In summary, our findings suggest that drought stress may enhance storage protein by regulating the expression of miRNAs and their target genes. (frontiersin.org)
  • Planctomycetes are also exceptional among Bacteria because they carry genes homologous to those coding for membrane coat (MC) proteins central to eukaryotic endocytosis ( 23 ). (pnas.org)
  • Three of these genes, that is, immune receptor translocation-associated protein 4 (IRTA4)/Fc receptor homologue 2 (FcRH2), angiopoietin 2 (ANGPT2) and Pim2 were selected for further validating studies in a cohort of 94 B-CLL patients. (broadinstitute.org)
  • The biochemical basis for recognition of dilysine motifs by coatomer has been controversial, but one path of research has led in recent years to a clear delineation of the dilysine motif‐binding sites. (embopress.org)
  • Mutations that affect the ER retention capacity of the motifs also abolished binding of the coatomer. (sciencemag.org)
  • The FL protein contains HEAT repeats and a C-terminal coiled coil domain that also contains multiple dibasic motifs, and ends in the dibasic motif RKLD-COOH. (wikipedia.org)
  • In addition, protein transport and lipid exchange often occur between LDs and various organelles to control lipid homeostasis in response to multiple stress responses and cellular signaling. (frontiersin.org)
  • Depending on the cellular requirements, the size, number, and protein content of these single membrane-bound organelles can vary widely. (mcponline.org)
  • In the "active" state, the GTP-bound GTPases interact with various downstream effector proteins that execute diverse cellular functions. (mdpi.com)
  • However, the mechanism by which protein aggregates can kill cells, or indeed, whether the presence of aggregates in diseased neurons is a cause or a consequence of underlying cellular pathology, has yet to be convincingly established. (rupress.org)
  • This pathway may also be used by cellular proteins, as deduced from our finding that TGN38 colocalized with the B-fragment on its transport from the plasma membrane to the TGN. (rupress.org)
  • Cellular retinol-binding protein-1 (CRBP-1) contributes to the maintenance of the differentiative state of endometrial cells through the regulation of bioavailability of retinol. (wikipedia.org)
  • Molecular cloning of two human cellular retinoic acid-binding proteins (CRABP). (wikipedia.org)
  • In this Cell Science at a Glance article and the accompanying poster, we discuss the unique features of Arf small G proteins, their functions in vesicular and lipid trafficking in cells, and how these functions are modulated by their regulators, the GEFs and GAPs. (biologists.org)
  • However, many misfolded proteins are targeted by covalent attachment of multiubiquitin chains for degradation by the proteasome ( Haas and Siepmann, 1997 ). (rupress.org)
  • Adaptins recognise and bind to clathrin through their hinge region (clathrin box), and recruit accessory proteins that modulate AP function through their C-terminal ear (appendage) domains. (wikipedia.org)
  • The protein has a divergent N-terminal kinase domain that is thought to be catalytically inactive, and can bind specific DNA sequences through its C-terminal domain. (wikipedia.org)
  • They also deliver to the pollen tube surface a wide variety of membrane, cell wall, and secretory proteins, including possible signaling molecules and hydrolytic enzymes that could be important for pollen tube growth. (plantcell.org)
  • However, little is known about the expression characteristics of miRNAs and how they regulate protein accumulation in wheat caryopsis under drought stress. (frontiersin.org)
  • Through association with merely ER resident proteins, in particular with proteins containing a reticulon homology domain, and with other peroxins, Pex30p designates peroxisome contact sites at ER subdomains. (mcponline.org)
  • There are three classes of Arf proteins in mammals, based largely on sequence homology - Class I (Arfs1-3), Class II (Arfs 4-5) and Class III (Arf6). (biologists.org)
  • Reduced Aβ production was not attributable to altered β-amyloid precursor protein (APP) ectodomain shedding but was a result of an enhanced degradation of APP C-terminal fragments (CTFs) in the absence of PAFAH1B2 but not its close homolog PAFAH1B3. (jneurosci.org)
  • It is unclear how the generation of Aβ is regulated, but potentially there are several steps along the pathway in which other proteins could intervene, such as with the activity of the secretase enzymes or the metabolic fate of Aβ and its immediate precursor the APP βCTF. (jneurosci.org)
  • Many of these protein families can be divided into subfamilies in which each paralogue performs a function similar to that of the other members but at a specific organellar location or in a distinct transport pathway ( Bonifacino and Glick, 2004 ). (biologists.org)
  • The first sorting station for correctly folded proteins in the secretory pathway is the ER exit site (ERES) ( Mezzacasa and Helenius, 2002 ), also called transitional ER. (biologists.org)
  • VIP36, an integral membrane protein previously isolated from epithelial MDCK cells, is an intracellular lectin of the secretory pathway. (biologists.org)
  • Proteins of the p24 family form a rather unique family of abundant, small (20-24 kDa) type I trans-membrane proteins in the early biosynthetic pathway. (biologists.org)
  • Functional enrichment and pathway analysis revealed that four pathways might be involved in storage protein biosynthesis. (frontiersin.org)
  • Under these conditions, the protein partitioned away from markers destined for the late endocytic pathway and colocalized extensively with cointernalized transferrin. (rupress.org)
  • The 58K protein has been identified as being FTCD , a bifunctional enzyme that channels 1-carbon units from formiminoglutamate, a metabolite of the histidine degradation pathway, to the folate pool. (acris-antibodies.com)
  • These results provide new insight into the relationship of enteroviruses with the components of the secretory pathway and on the role of SVDV 2C protein in this process. (frontiersin.org)