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.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 188.8.131.52.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)Electron Transport Complex I: 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 184.108.40.206.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.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.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.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)Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.Research Support, Non-U.S. Gov'tResearch Support, U.S. GovernmentResearch Support, American Recovery and Reinvestment ActFacility Design and Construction: Architecture, exterior and interior design, and construction of facilities other than hospitals, e.g., dental schools, medical schools, ambulatory care clinics, and specified units of health care facilities. The concept also includes architecture, design, and construction of specialized contained, controlled, or closed research environments including those of space labs and stations.Research Support, N.I.H., ExtramuralBibliometrics: The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)Publications: Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)Barth Syndrome: Rare congenital X-linked disorder of lipid metabolism. Barth syndrome is transmitted in an X-linked recessive pattern. The syndrome is characterized by muscular weakness, growth retardation, DILATED CARDIOMYOPATHY, variable NEUTROPENIA, 3-methylglutaconic aciduria (type II) and decreases in mitochondrial CARDIOLIPIN level. Other biochemical and morphological mitochondrial abnormalities also exist.Butylene Glycols: 4-carbon straight chain aliphatic hydrocarbons substituted with two hydroxyl groups. The hydroxyl groups cannot be on the same carbon atom.Research: Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)Publishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.Foxes: Any of several carnivores in the family CANIDAE, that possess erect ears and long bushy tails and are smaller than WOLVES. They are classified in several genera and found on all continents except Antarctica.Dictionaries, MedicalDictionaries as Topic: Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.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 220.127.116.11Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Stem Cell Research: Experimentation on STEM CELLS and on the use of stem cells.Brefeldin A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.Bambusa: A plant genus of the family POACEAE. Young shoots are eaten in Asian foods while the stiff mature stems are used for construction of many things. The common name of bamboo is also used for other genera of Poaceae including Phyllostachys, SASA, and Dendrocalamus.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Posters as Topic: Single or multi-sheet notices made to attract attention to events, activities, causes, goods, or services. They are for display, usually in a public place and are chiefly pictorial.Gold: A yellow metallic element with the atomic symbol Au, atomic number 79, and atomic weight 197. It is used in jewelry, goldplating of other metals, as currency, and in dental restoration. Many of its clinical applications, such as ANTIRHEUMATIC AGENTS, are in the form of its salts.Metal Nanoparticles: Nanoparticles produced from metals whose uses include biosensors, optics, and catalysts. In biomedical applications the particles frequently involve the noble metals, especially gold and silver.Gold Colloid: A suspension of metallic gold particles.Microscopy, Electron, Transmission: Electron microscopy in which the ELECTRONS or their reaction products that pass down through the specimen are imaged below the plane of the specimen.Particle Size: Relating to the size of solids.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.-.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.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Amino Acid Sequence: 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.Systems Integration: The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Thermotoga maritima: A rod-shaped bacterium surrounded by a sheath-like structure which protrudes balloon-like beyond the ends of the cell. It is thermophilic, with growth occurring at temperatures as high as 90 degrees C. It is isolated from geothermally heated marine sediments or hot springs. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Databases, Genetic: Databases devoted to knowledge about specific genes and gene products.Genome, Human: The complete genetic complement contained in the DNA of a set of CHROMOSOMES in a HUMAN. The length of the human genome is about 3 billion base pairs.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).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.Genes: A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.
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 . In mammalian cells, these vesicles coalesce to form tubulo-vesicular transport complexes (TCs), which shuttle anterograde cargo from the ER to the Golgi complex   . In contrast, COPI-coated vesicles are proposed to mediate recycling of proteins from the Golgi complex to the ER    . The binding of COPI to COPII-coated TCs   , however, has led to the proposal that COPI binds to TCs and specifically packages recycling proteins into retrograde vesicles for return to the ER  . 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  , 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  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)
Vesicular transport protein
Cytosolic coat protein complex ) : retrograde transport ; Golgi ----> Endoplasmic reticulum COP 2 (Cytosolic coat protein ... Examples include: Archain ARFs Clathrin Caveolin Dynamin and related proteins, such as the EHD protein family Rab proteins ... A vesicular transport protein, or vesicular transporter, is a membrane protein that regulates or facilitates the movement of ... Sorting nexins Synaptotagmin TRAPP complex Synaptophysin Auxilin There are multiple pathways, each using its own coat and ...
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 ... "Sec24 proteins and sorting at the endoplasmic reticulum". J Biol Chem. 274 (12): 7833-40. doi:10.1074/jbc.274.12.7833. PMID ...
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 ...
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 ...
... refers to the specific coat protein complex that initiates the budding process. The coat consists of large protein subcomplexes ... There are two protein heterodimers that form the coat complex. These proteins are Sec23p/Sec24p Heterodimer Sec13p/Sec31p ... COPII is a coatomer, a type of vesicle coat protein that transports proteins from the rough endoplasmic reticulum to the Golgi ... The pre-budding complex recruits the long, flexible Sec13p/31p complex. Sec13p/31p complexes polymerizes on the cytosolic side ...
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". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/ ...
... is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to ... refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of ... 1. Luminal proteins: Proteins found in the lumen of the Golgi complex that need to be transported to the lumen of the ER ... COPII vesicles Clathrin vesicles Glyceraldehyde 3-phosphate dehydrogenase#ER to Golgi transport Exomer Coat Protein Complex I ...
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 ...
Adaptor-related protein complex 2, alpha 1
The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in ... This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles ... Adaptor-related protein complex 2, alpha 1 has been shown to interact with DPYSL2 and NUMB. GRCh38: Ensembl release 89: ... AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene. ...
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 ... 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 ...
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- ...
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 ...
Coiled-coil domain containing 115
... and coat protein complex I (COPI) vesicles in some human cells. The encoded protein shares some homology with the yeast V- ... Coiled-coil domain containing 115 is a protein that in humans is encoded by the CCDC115 gene. The protein encoded by this gene ... "CCDC115 Deficiency Causes a Disorder of Golgi Homeostasis with Abnormal Protein Glycosylation". Am. J. Hum. Genet. 98 (2): 310- ... ATPase assembly factor Vma22p, and the orthologous protein in mouse promotes cell proliferation and suppresses cell death. ...
... reticulons may be used to shape coated protein vesicles by interacting with a component of the adaptor protein complex (which ... The family of vertebrate proteins are called reticulons, and all other located eukaryotes are called reticulon-like proteins. ... The first reticulon protein RTN1 was characterized as an antigen for neuroendocrine cells from a cDNA in neural tissue. It was ... One way those proteins can be compared to reticulons is in looking at reticulon-depleted yeast cells. Fluorescence was detected ...
This technique is still a particularly valuable for very large protein complexes such as virus coat proteins and amyloid fibers ... The sequence of a protein is unique to that protein, and defines the structure and function of the protein. The sequence of a ... For larger protein complexes, cryo-electron microscopy can determine protein structures. The resolution is typically lower than ... proteins is considered evidence of evolutionary relatedness between proteins and is used group proteins together into protein ...
Field, Mark C.; Sali, Andrej; Rout, Michael P. (13 June 2011). "On a bender-BARs, ESCRTs, COPs, and finally getting your coat ... The peridinin-chlorophyll-protein complex (PCP or PerCP) is a soluble molecular complex consisting of the peridinin-chlorophyll ... Whether formed from a protein monomer or dimer, the assembled protein-pigment complex is sometimes known as bPCP (for "building ... They additionally contain water-soluble protein-pigment complexes that exploit carotenoids such as peridinin to extend their ...
Clathrin adaptor protein
Adaptor protein (AP) 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- ... AP2 adaptor complex associates with the plasma membrane and is responsible for endocytosis. AP3 is responsible for protein ...
Ras-associated protein 1 recruits this protein to coat protein complex II (COPII) vesicles during budding from the endoplasmic ... Barr FA, Nakamura N, Warren G (1998). "Mapping the interaction between GRASP65 and GM130, components of a protein complex ... The protein encoded by this gene is a peripheral membrane protein which recycles between the cytosol and the Golgi apparatus ... "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome ...
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. ...
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. ...
... where it serves as the binding site for the Sec23/Sec24 protein coat complex. After the vesicle coat is completely assembled ... SAR1A or Sar1 is a protein involved in membrane trafficking. It is a monomeric small GTPase found in COPII vesicles. It ... which triggers the disassembly of the COPII coat. ARF. ... regulates the assembly and disassembly of COPII coats. GDP- ...
... which is composed of chitin and protein complex. This protects the parasites from the digestive enzymes of the host. The ... The stages of development in sandfly can be described as follows: Soon after entering the gut, the amastigotes get coated with ... L. donovani is now considered to be a complex species as indicated by different pathological symptoms occurring in different ... DNA sequencing of different geographical strains indicates that the protozoan complex can be classified into two valid taxons, ...
Adaptor protein complex 1 is found at the cytoplasmic face of coated vesicles located at the Golgi complex, where it mediates ... The protein encoded by this gene serves as one of the large subunits of this complex and is a member of the adaptin protein ... AP-1 complex subunit beta-1 is a protein that in humans is encoded by the AP1B1 gene. ... "Entrez Gene: AP1B1 adaptor-related protein complex 1, beta 1 subunit". Nakagawa, T; Setou M; Seog D; Ogasawara K; Dohmae N; ...
Another was that the virus coat, the protein capsid, is dependent upon the genetic material in the RNA core of the particle and ... to study the structures of large macromolecular complexes. 2006 marked the publication of Schulten's model of the LH2 structure ... This suggests that the genetic material must already be present before the virus can build its coat when reproducing. Such ... His work made possible the dynamic simulation of the activities of thousands of proteins working together at the macromolecular ...
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., ...
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.
COPI vesicles accumulating in the presence of a GTP restricted arf1 mutant are depleted of anterograde and retrograde cargo |...
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 ...
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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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。
A Rubicon t rt nelmi foly irat honlapja. A tartalma szerint tudom nyos ismeretterjeszt foly irat magazinszer en n pszer s ti a t rt nelmet. Ahogy az iskol ban nem hallhatta...
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 18.104.22.168 ...
COPI-mediated membrane trafficking is required for cytokinesis in Drosophila male meiotic divisions | Journal of Cell Science
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 ...
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 ...
北京大学医学部机构知识库([email protected]): Cloning, expression and biochemical activity of ARFGAP3, a regulator of intracellular transport
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.
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.
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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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 ...
Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.
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Monoklonale und polyklonale ARFGAP3 Antikörper für viele Methoden. Ausgesuchte Qualitäts-Hersteller für ARFGAP3 Antikörper. Hier bestellen.
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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 ...
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.
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
RebornData asks: Thanks to a move and continuing instability in the DSL market, Im now the proud owner of three DSL modems of various types gathering dust in my closet. Its a sordid tale. While I know that obselete hardware is worth next to nothing, this hardware isnt necessarily obselete, wit...
ARFGAP1 recombinant protein | ADP-ribosylation factor GTPase-activating protein 1 (ARFGAP1) Recombinant Protein-NP 001268411.1
Buy ARFGAP1 recombinant protein, ADP-ribosylation factor GTPase-activating protein 1 (ARFGAP1) Recombinant Protein-NP_001268411.1 (MBS1301288) product datasheet at MyBioSource, Recombinant Proteins
As the debate surrounding the telcos has lately been focused on net neutrality, another issue that is a result of the lack of competition in the space has slipped back under the radar: naked DSL. Most of the telcos (Qwest being a notable exception) require that any customer who wants a DSL line also has to buy phone service from them as well. This is what allows them to claim they charge only $15 or whatever for a DSL line, but if you add in the phone service and additional fees it tends to be much higher. Its never made much sense that the telcos are so against just offering plain old naked DSL without the phone service. After all, for people who just want to use a mobile phone and/or VoIP, isnt that only going to encourage them to go to the competition who wont force them to bundle an unwanted service? Oh... right. There isnt much competition, which is what allows the telcos to get away with the bundle. For quite some time, theres been some pressure on SBC/AT&T to offer naked DSL in ...
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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 ...
The cell. 5. Vesicular trafficking. From the reticulum to the Golgi. Atlas of plant and animal histology.
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 ...
Peng, R.; Grabowski, R.; De Antoni, A.; Gallwitz, D.: Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles. Proceedings of the National Academy of Sciences USA 96, pp. 3751 - 3756 (1999 ...
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Cant seem to find another appropriate place or this question so I appologize if it is the wrong forum.. After I do DSL HD install, it boots up GREAT! No issue there. But I want to update to a custom 2.6 kernel... So I install a second HD, boot Knoppix and compile a new kernel modules etc. Now I have "bzImage2.6" and "22.214.171.124" modules.. I copied the files over to the HD where the DSL installation is (hda1) and modify /dev/hda1 -> /etc/lilo.conf to point to bzImage2.6 and rerun lilo.. It hangs after lilo.. What did I do wrong and can someone point me to some doc of how to update the kernel for DSL after HD-DSL installation... ...
Affiliation：千葉大学,医学部,助手, Research Field：Dermatology, Keywords：デコリン,デルマトポンチン,強皮症,細胞外マトリックス,コラーゲン,transcription,cutis laxa,転写,I型コラーゲン,皮膚線維症, # of Research Projects：10, # of Research Products：0
Learn what others have been doing with the DSL Tools to create their own graphical or form-based designers, and learn how to create your own using the DSL Tools for Visual Studio 2010.
Tube Expansion Deformation Enables In Situ Synchrotron X-ray Scattering Measurements during Extensional Flow-Induced...
2018 The Author(s). Licensee MDPI, Basel, Switzerland. This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0). Received: 11 February 2018 / Revised: 4 March 2018 / Accepted: 6 March 2018 / Published: 8 March 2018. (This article belongs to the Special Issue Processing-Structure-Properties Relationships in Polymers) This research used resources of the Advanced Photon Source (APS), a US Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract DE-AC02-06CH11357. The authors acknowledge all the staff at beamline 5-ID-D DND-CAT of the Advanced Photon Source (APS) at the Argonne National Laboratories, especially Steven Weigand and James Rix for their support before and during the synchrotron experiments. The authors acknowledge Mary Beth Kossuth at ...
This antibody pair set comes with matched antibody pair to detect and quantify protein level of human SCYL3. (H00057147-AP21) - Products - Abnova
(His)6-GBF1 is a BFA-resistant ARF-GEF. (A) Fractions enriched in (His)6-GBF1 display a GEF specific for ARFs. Identical volumes (5 μl) of the 50 mM imidazole
Poodles have a rather unusual coat. It has the appearance of puppy hair and is quite curly. To keep your precious poodles coat shiny and healthy, brush it daily, clip it monthly, choose a ...
The Australian Open has been hit hard by absences with Andy Murray, Serena Williams and Kei Nishikori among those to have withdrawn, while Nadal and Novak Djokovic have also been struggling with injuries. ...
Structural Component Of 3 Distinct Complexes; Subunit Of Nup84 Nuclear Pore Sub-complex (NPC), COPII Vesicle Coat, And Seh1-associated (SEA) Complex; COPII Vesicle Coat Is Required For ER To Golgi Transport; The Nup84 Subcomplex Contributes To Nucleocytoplasmic Transport, NPC Biogenesis And Processes That May Require Localization Of Chromosomes At The Nuclear Periphery, Including Transcription; Homologous To Human SEC13; Abundance Increases Under DNA Replication Stress
Compare & find the top performing anti-Rat (Rattus) ARFGAP1 antibody for Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)).
The final volume of Love in Focus is here! After the dramatic events of Volume 2, just who will our heroine end up dating (if anyone)? Everything is at stake, and friendships are muddled, as our protagonist comes to grips with her feelings… At the end of Volume 2 Mako was confessed to by childhood friend Kei, whom weve long known has had a crush on her. His confession is such a shock to Mako that she comes down with a fever! After recovering, she spends a week mulling over Keis words, debating if she sees him as a romantic interest or not. In the end Kei suggests that he and Mako begin dating on a trial basis, to see how things go. Mako agrees to this but its clear to Kei that her feelings arent necessarily in his favour. Elsewhere, Amemura is upset by news of Mako and Kei becoming a couple, but he tells Kei he has no intention of stealing her from him. Its an honest and noble comment from the more likeable love interest of the two. When not knee-deep in the romance, this volume of Love ...
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So what are the keys to a healthy and beautiful coat, and what should you do if your dog or cat is starting to look a little mangy? Here, find everything you need to know about year-round coat care for your pet.
Au început lucrarile la noul corp de sase etaje al Spitalului Clinic de Copii Victor Gomoiu, primul spital universitar de urgenta pentru copii construit în Bucuresti în ultimii 30 de ani. Demararea lucrarilor a fost marcata, vineri,...
مجموعه جی.کوت در سال 1393 به پشتوانه بیش از 20 سال ارایه خدمات در صنعت خودرو، فعالیت خود را به صورت کاملن تخصصی در زمینه دیتیلینگ خودرو آغاز نموده است .با همراهی و نگاه حمایت گر شما توانسته است پس از مدت کوتاهی خود را به عنوان یکی از بزرگترین و خوشنامترین فعالان حوزه دیتیلینگ در ایران معرفی نماید. ...
ADP ribosylation factor 6 regulates neuronal migration in the developing cerebral cortex through FIP3/arfophilin-1-dependent...
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 ...
L-type lectins possess a luminal carbohydrate recognition domain (CRD) that binds to high-mannose-type oligosaccharides in aCa2+-dependent manner. The L-type CRD is named after the lectins found in...
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（後來在真核細胞中也證實此結構的存在）。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。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 ...
ARFGAP3 antibody, C-term (ADP-ribosylation factor GTPase activating protein 3) for WB. Anti-ARFGAP3 pAb (GTX89988) is tested in Mouse samples. 100% Ab-Assurance.
Cellular processesCellular processesSporulation and germinationspore coat assembly protein SafA (TIGR02899; HMM-score: 63.9) ...
... : medicina copii, medicina de copii, femeile aflate la menopauza, tratamentul bolilor, efecte benefice, tulburari de menopauza, dermatologie, mici interventii chirurgicale, tratament acnee, afectiuni...
JoVE Search Results: Coat Protein Complex Coated Vesicles
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 ...http://labindex.jove.com/group/Coat-Protein-Complex-Coated-Vesicles
Luteolin decreases the yield of influenza A virus in vitro by interfering with the coat protein I complex expression |...
Luteolin decreases the yield of influenza A virus in vitro by interfering with the coat protein I complex expression. ... Luteolin decreases the yield of influenza A virus in vitro by interfering with the coat protein I complex expression ... In addition, we found that luteolin suppressed coat protein I complex expression, which was related to influenza virus entry ... Zurück zum Zitat Sun E, He J, Zhuang X (2013) Dissecting the role of COPI complexes in influenza virus infection. J Virol 87: ...https://www.springermedizin.de/luteolin-decreases-the-yield-of-influenza-a-virus-in-vitro-by-in/16469110
RCSB PDB - 3EGD: Crystal structure of the mammalian COPII-coat protein Sec23a/24a complexed with the SNARE protein Sec22 and...
Crystal structure of the mammalian COPII-coat protein Sec23a/24a complexed with the SNARE protein Sec22 and bound to the ... Crystal structure of the mammalian COPII-coat protein Sec23a/24a complexed with the SNARE protein Sec22 and bound to the ... Structural basis of cargo membrane protein discrimination by the human COPII coat machinery.. Mancias, J.D., Goldberg, J.. ( ... a framework to understand how an expansion of coat subunits extends the range of cargo proteins packaged into COPII-coated ...https://www.rcsb.org/structure/3EGD
RCSB PDB - 1U1Y: Crystal structure of a complex between WT bacteriophage MS2 coat protein and an F5 aptamer RNA...
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 ...http://www.rcsb.org/pdb/explore/explore.do?structureId=1U1Y
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 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 ...https://www.deepdyve.com/lp/springer_journal/chaperone-protein-grpe-and-the-groel-groes-complex-promote-the-correct-094B8SRNZR
β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular Stomatitis...
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 ...https://rd.springer.com/chapter/10.1007/978-3-662-02928-2_26
Organization of the ER-Golgi interface for membrane traffic control. - PubMed - NCBI
Coat protein complex II (COPII)-coated vesicles originate within cup-shaped ER subdomains, which are associated with the plus ... Coat protein complex I (COPI) and COPII are required for bidirectional membrane trafficking between the endoplasmic reticulum ( ... Structural analyses have demonstrated that the coat protein complex II (COPII) cage, which consists of the SEC13-SEC31 and ... as well as uncoating and fusion of coat protein complex II (COPII) and COPI carriers with their respective compartments. These ...https://www.ncbi.nlm.nih.gov/pubmed/23698585
Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking | JCB
The formation of coat protein complex I (COPI)-coated vesicles is regulated by the small guanosine triphosphatase (GTPase) ... coat protein complex; GAP, GTPase-activating protein; NRK, normal rat kidney. ... Coat protein complex I (COPI) vesicles are involved in transport processes within the early secretory pathway (Bethune et al., ... The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3. J. Cell Sci. 118:3555-3566. ...http://jcb.rupress.org/content/183/4/725
N-Glycosylation is required for FDNC5 stabilization and irisin secretion | Biochemical Journal
protein trafficking. *. Abbreviations. AA, amino acid; CHX, cycloheximide; COP, coat protein complex; DMEM, Dulbeccos modified ... fibronectin type III domain-containing protein 5; GFP, green fluorescent protein; PNGase F, peptide:N-glycosidase F; RIPA, ... enhanced green fluorescent protein; Endo H, endoglycosidase H; ER, endoplasmic reticulum; FNDC5, ...http://www.biochemj.org/content/474/18/3167
Requirements for Transitional Endoplasmic Reticulum Site Structure and Function in Saccharomyces cerevisiae
Coat protein complex II (COPII) proteins are enriched at tER sites, although the mechanisms underlying tER site assembly and ... coat protein complex II. DTT. dithiothreitol. PC-PLC. phosphatidylcholine phospholipase C. PI. phosphatidylinositol. PI-PLC. ... Kapetanovich L., Baughman C., Lee T. H. Nm23H2 facilitates coat protein complex II assembly and endoplasmic reticulum export in ... Peng R., De Antoni A., Gallwitz D. Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p ...http://pubmedcentralcanada.ca/pmcc/articles/PMC2861612/?lang=en-ca
Produktübersicht anti-AP3B2 Antikörper
Protein Überblick Adaptor protein-3 (AP3) is a heterotetrameric vesicle-coat protein complex. Some AP3 subunits are ... anti-Adaptor-Related Protein Complex 1 Associated Regulatory Protein Antikörper * anti-Adaptor Related Protein Complex 4 sigma ... clathrin assembly protein complex 3 beta-2 large chain , neuron-specific vesicle coat protein beta-NAP , AP-3 complex beta-2 ... Neuronal adaptin-like protein, beta-subunit , adapter-related protein complex 3 subunit beta-2 , adaptor protein complex AP-3 ...https://www.antikoerper-online.de/abstract/Adaptor-Related+Protein+Complex+3%2C+beta+2+Subunit+
The presence of an ER exit signal determines the protein sorting upon ER exit in yeast | Biochemical Journal
glycosylphosphatidylinositol-anchored protein. Abbreviations: ALP, alkaline phosphatase; COPII, coat protein complex II; DRM, ... We attempted to identify sorting determinants for this protein sorting event in the ER. We found that mutant Gas1 proteins that ... we conclude that DRM partitioning of GPI-anchored proteins is not the dominant determinant of protein sorting upon ER exit. ... The presence of an ER exit signal determines the protein sorting upon ER exit in yeast. Reika Watanabe, Guillaume A. Castillon ...http://www.biochemj.org/content/414/2/237
Vesicular transport protein - Wikipedia
Cytosolic coat protein complex ) : retrograde transport ; Golgi -- Endoplasmic reticulum COP 2 (Cytosolic coat protein ... Examples include: Archain ARFs Clathrin Caveolin Dynamin and related proteins, such as the EHD protein family Rab proteins ... A vesicular transport protein, or vesicular transporter, is a membrane protein that regulates or facilitates the movement of ... Sorting nexins Synaptotagmin TRAPP complex Synaptophysin Auxilin There are multiple pathways, each using its own coat and ...https://en.wikipedia.org/wiki/Vesicular_transport_protein
Frontiers | Activators and Effectors of the Small G Protein Arf1 in Regulation of Golgi Dynamics During the Cell Division Cycle...
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 ...https://www.frontiersin.org/articles/10.3389/fcell.2018.00029/full
Rerouting the traffic from a virus perspective
... protein complexes. Both complexes are involved in clathrin-dependent trafficking. In addition to these coats, Arf proteins also ... Protein 2C disrupts the Golgi but has no apparent effect on protein secretion (12, 48). Conversely, protein 2B inhibits protein ... The Arf-related GTPase Sar1 regulates coat protein complex II (COPII). COPII consists of Sec23, Sec24, Sec13 and Sec31, which ... Viral proteins recruit and interact with cellular trafficking proteins to divert the normal trafficking of key proteins or to ...http://www.bioscience.org/2017/v22/af/4575/2.htm
Ingolf Bach's research topics | Profiles RNS
Coat Protein Complex I. 1. 2011. 1. 0.140. Why? Muscular Atrophy, Spinal. 1 ...https://profiles.umassmed.edu/display/133506/network/researchareas/details
Hong-Gang Wang, PhD - Research Output - Penn State
... mediates macroautophagy by interacting with beclin1-containing autophagy protein complex. Niu, G., Zhang, H., Liu, D., Chen, L ... Autophagosomal membrane serves as platform for intracellular death-inducing signaling complex (iDISC)-mediated caspase-8 ... coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex. He ... FRET and NMR analyses reveal selective binding of peptides containing the LC3-interacting region to ATG8 family proteins. ...https://pennstate.pure.elsevier.com/en/persons/hong-gang-wang/publications/?type=%2Fdk%2Fatira%2Fpure%2Fresearchoutput%2Fresearchoutputtypes%2Fcontributiontojournal%2Farticle
ITSN | SpringerLink
Ese; Intersectin The Intersectin family refers to a group of proteins that share N-terminal EH domains, a central coiled-coil ... The transmitter release-site CaV2.2 channel cluster is linked to an endocytosis coat protein complex. Eur J Neurosci. 2007;26(3 ... Fractional recovery analysis of a presynaptic synaptotagmin 1-anchored endocytic protein complex. PLoS One. 2006;1:e67.PubMed ... Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits. Dev Cell. 2009;17(6):811- ...https://link.springer.com/referenceworkentry/10.1007%2F978-3-319-67199-4_440
Rab GTPases and membrane identity: Causal or inconsequential? | JCB
A) Discrete coat protein complexes (green) recruit the first group. For example, COP II recruits the Rab1 GEF TRAPP to ER-Golgi ... Recent data on the structure of Rab GTPase regulators and coat protein complexes has identified common features with GTPase ... The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein. J. ... vesicle coat protein complexes, and the MglA GTPase-MglB bacterial cell polarity regulator (Sun et al., 2007; Miertzschke et al ...http://jcb.rupress.org/content/202/2/191
SBNet - Publications
Structural basis of pyrimidine specificity in the MS2 RNA hairpin-coat-protein complex.. RNA 7, 1616-1627.. (PubMed) *Hansson H ... Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins.. Acta ... Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids.. Acta Cryst. D55, 1850-1857 ... Investigating the structural basis of purine specificity in the structures of MS2 coat protein RNA translational operator ...http://xray.bmc.uu.se/sbnet/publications.html
SEC24B - Wikipedia
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 ... "Sec24 proteins and sorting at the endoplasmic reticulum". J Biol Chem. 274 (12): 7833-40. doi:10.1074/jbc.274.12.7833. PMID ...https://en.wikipedia.org/wiki/SEC24B
AP2M1 - AP-2 complex subunit mu - Homo sapiens (Human) - AP2M1 gene & protein
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 ...https://www.uniprot.org/uniprot/Q96CW1
The COPII pathway and hematologic disease | Blood Journal
... a component of coat protein complex II (COPII)-coated vesicles that bud from the surface of the ER and transport cargo proteins ... CDAII is caused by mutations in the SEC23B gene, which encodes a core component of the coat protein complex II (COPII). F5F8D ... Erv26p directs pro-alkaline phosphatase into endoplasmic reticulum-derived coat protein complex II transport vesicles. Mol Biol ... COPII coat proteins in higher eukaryotes. The COPII proteins are evolutionarily conserved; orthologs of the core components of ...http://www.bloodjournal.org/content/120/1/31?ijkey=b7b50be634130f63be32da4efaa22f40ec5de0b2&keytype2=tf_ipsecsha&sso-checked=true
The COPII pathway and hematologic disease | Blood Journal
... a component of coat protein complex II (COPII)-coated vesicles that bud from the surface of the ER and transport cargo proteins ... CDAII is caused by mutations in the SEC23B gene, which encodes a core component of the coat protein complex II (COPII). F5F8D ... Erv26p directs pro-alkaline phosphatase into endoplasmic reticulum-derived coat protein complex II transport vesicles. Mol Biol ... COPII coat proteins in higher eukaryotes. The COPII proteins are evolutionarily conserved; orthologs of the core components of ...http://www.bloodjournal.org/content/120/1/31?ijkey=425ca81fee0a96d55ac0ee811b59c4abc336d931&keytype2=tf_ipsecsha&sso-checked=true
Table of Contents - September 15, 1998, 95 (19) | PNAS
Coatomer, Arf1p, and nucleotide are required to bud coat protein complex I-coated vesicles from large synthetic liposomes * ... Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21CIP1/WAF1 and cyclin D proteins Zhong-Kang Yu, Jennifer L. M ... DNA sequence-dependent deformability deduced from protein-DNA crystal complexes Wilma K. Olson, Andrey A. Gorin, Xiang-Jun Lu, ... Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex Michael E. Hurwitz, ...http://www.pnas.org/content/95/19
VesiclesCOPIIGolgiMammalianEndoplasmicCytosolicCargoVesicular transportSubunitsSubunitYeastVesicle-coatPathwaysMediated by vesicularDynaminMembranesEffectorELISA KitsReceptorClathrin-mediated endocytosisVitroGTPasesEndocytosisScaffoldEukaryoticSecretoryEndocyticSec24UniProtGAPsNucleotideNeuronsBacteriophageConformationalRecruitSaccharomyces
- Thus, the human genome encodes four forms of Sec24, the cargo selection subunit of the COPII vesicular coat, and this is proposed to increase the range of cargo accommodated by human COPII-coated vesicles. (rcsb.org)
- A comparative analysis of crystal structures of the four human Sec24 isoforms establishes the structural determinants for discrimination among these transport signals, and provides a framework to understand how an expansion of coat subunits extends the range of cargo proteins packaged into COPII-coated vesicles. (rcsb.org)
- 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)
- Scheel J, Kreis TE (1991) Motor protein independent binding of endocytic carrier vesicles to microtubules in vitro. (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)
- 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)
- Arf GTPase-activating protein (GAP) catalyzed GTP hydrolysis in Arf1 triggers uncoating and is required for uptake of cargo molecules into vesicles. (rupress.org)
- 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)
- 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)
- Furthermore, a mutant glycosylated α-factor, gpαGPI, which contains both the GPI anchor and S/T region from Gas1p, still entered Gap1p-containing vesicles, demonstrating that these conserved characteristics do not prevent proteins from entering Gap1p-containing vesicles. (biochemj.org)
- Based on the fact that they entered different ER-derived vesicles, we conclude that DRM partitioning of GPI-anchored proteins is not the dominant determinant of protein sorting upon ER exit. (biochemj.org)
- Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. (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)
- 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)
- 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)
- Transport of secretory and membrane cargo proteins is mediated by diffusible vesicles. (berkeley.edu)
- The formation of these vesicles in vitro depends on the Sec proteins that were predicted to be involved from genetic and morphological inspection of sec mutant cells. (berkeley.edu)
- 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)
- This coat (COPII) resembles another coat complex (COPI) that creates transport vesicles within the Golgi apparatus. (berkeley.edu)
- A model for the binding of coat proteins and capture of membrane molecules in COPII vesicles. (berkeley.edu)
- 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)
- Contributors examine how proteins translocate across the ER membrane, the processes that occur inside the ER lumen (e.g., folding, glycosylation, and disulfide bond formation), and how the proteins are packaged into vesicles and transported to the Golgi. (cshlpress.com)
- Coat protein complex I (COPI) and COPII are required for bidirectional membrane trafficking between the endoplasmic reticulum (ER) and the Golgi. (nih.gov)
- Bidirectional transport of secretory cargo between the endoplasmic reticulum (ER) and the Golgi requires budding, movement, tethering, as well as uncoating and fusion of coat protein complex II (COPII) and COPI carriers with their respective compartments. (nih.gov)
- Structural analyses have demonstrated that the coat protein complex II (COPII) cage, which consists of the SEC13-SEC31 and SEC23-SEC24 subcomplexes, has a flexible architecture. (nih.gov)
- 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)
- CDAII is caused by mutations in the SEC23B gene, which encodes a core component of the coat protein complex II (COPII). (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)
- 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)
- 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)
- 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 encoded protein has similarity to yeast Sec24p component of COPII. (bio-rad.com)
- COPII is the coat protein complex responsible for vesicle budding from the ER. (bio-rad.com)
- 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, (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)
- While these core coat machineries and other transport factors are highly conserved across species, high-resolution imaging studies indicate that the organization of the ER-Golgi interface is varied in eukaryotic cells. (nih.gov)
- 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)
- 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)
- 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)
- 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)
- Genomic analysis shows that the increased complexity of trafficking pathways in mammalian cells involves an expansion of the number of SNARE, Rab and COP proteins. (rcsb.org)
- 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)
- 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)
- Secretory proteins are exported from the endoplasmic reticulum (ER) at specialized regions known as the transitional ER (tER). (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)
- For example, the endoplasmic reticulum (ER) is a neutral pH, reducing environment containing chaperones conducive to protein folding and the formation of disulfide bonds, whereas the lysosomes are ∼pH 5 and contain catabolic enzymes maximally active at acidic pH. (rupress.org)
- The endoplasmic reticulum (ER) is an extensive network of membranes that folds, modifies, and transports proteins in eukaryotic cells. (cshlpress.com)
- Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. (uniprot.org)
- AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. (uniprot.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)
- 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)
- 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)
- Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. (nih.gov)
- AP2 (zeige GTF3A ELISA Kits ) has evolved as a key regulatory node to coordinate clarhtin-coated pit (zeige IRF6 ELISA Kits ) formation and cargo sorting and ensure high spatial and temporal regulation of cathrin-mediated endocytosis. (antikoerper-online.de)
- Results indicate that AP-2 is not essential for clathrin -coated vesicle formation at the plasma membrane, but that it is one of several endocytic adaptors required for the uptake of certain cargo proteins. (antikoerper-online.de)
- 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)
- 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)
- 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)
- They control the vesicular transport of proteins in different trafficking pathways (PubMed:10066790, PubMed:10436028). (nih.gov)
- DellAngelica, Ooi, Bonifacino: Beta3A-adaptin, a subunit of the adaptor-like complex AP-3. (antikoerper-online.de)
- Autosomal-Recessive Mutations in AP3B2 , Adaptor-Related Protein Complex 3 Beta 2 Subunit , Cause an Early-Onset Epileptic Encephalopathy with Optic Atrophy. (antikoerper-online.de)
- Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the F1 antigen Caf1M-Caf1 chaperone-subunit pre-assembly complex from Yersinia pestis . (uu.se)
- 171 Adaptor-Related Protein Complex 2, mu 1 Subunit (AP2M1) Antibodies from 23 manufacturers are available on www.antibodies-online.com. (antibodies-online.com)
- Auf www.antikoerper-online.de finden Sie aktuell 17 Adaptor-Related Protein Complex 2, mu 1 Subunit (AP2M1) ELISA Kits von 5 unterschiedlichen Herstellern. (antikoerper-online.de)
- Zusätzlich bieten wir Ihnen Adaptor-Related Protein Complex 2, mu 1 Subunit Antikörper (150) und Adaptor-Related Protein Complex 2, mu 1 Subunit Proteine (16) und viele weitere Produktgruppen zu diesem Protein an. (antikoerper-online.de)
- Insgesamt sind aktuell 191 Adaptor-Related Protein Complex 2, mu 1 Subunit Produkte verfügbar. (antikoerper-online.de)
- Arkadia (zeige RNF111 ELISA Kits ) complexes with clathrin adaptor AP2 (zeige GTF3A ELISA Kits ) mu2 subunit and regulates EGF (zeige EGF ELISA Kits ) signalling. (antikoerper-online.de)
- Schekman R (1985) Protein localization and membrane traffic in yeast. (springer.com)
- Basic principles that emerged from these studies in yeast are now being applied to studies of genetic diseases of protein transport. (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)
- Though valuable, this organization requires some form of active transport machinery for the exchange of material between these compartments because large hydrophilic molecules such as proteins cannot easily cross membranes. (rupress.org)
- Tethering is a less well-defined event involving the Rab GTPases and effector protein complexes, typically large extended molecules thought to bridge the space between two approaching membranes ( Gillingham and Munro, 2003 ). (rupress.org)
- 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 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)
- Search, Find and Buy Antibodies, ELISA Kits and Proteins. (antibodies-online.com)
- BMCC1 (zeige PRUNE2 ELISA Kits ) is an AP-2 (zeige GTF3A ELISA Kits ) associated endosomal protein in prostate cancer cells. (antikoerper-online.de)
- These results suggest that AP-2 (zeige GTF3A ELISA Kits ) is essential for endocytic clathrin coated- pit (zeige IRF6 ELISA Kits ) and coated-vesicle formation. (antikoerper-online.de)
- In addition, we found that luteolin suppressed coat protein I complex expression, which was related to influenza virus entry and endocytic pathway. (springermedizin.de)
- Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP. (springer.com)
- Fractional recovery' analysis of a presynaptic synaptotagmin 1-anchored endocytic protein complex. (springer.com)