Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants. [PDF]
PLoS ONE, 2012 Retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) depends on the formation of vesicles coated with the multiprotein complex COPI.
Katarzyna Jarmoszewicz +3 more
doaj +7 more sources
Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. [PDF]
The Journal of cell biology, 1993 The cycle of nucleotide exchange and hydrolysis by a small GTP-binding protein, ADP-ribosylation factor (ARF), helps to provide vectoriality to vesicle transport. Coat assembly is triggered when ARF binds GTP, initiating transport vesicle budding, and coat disassembly is triggered when ARF hydrolyzes GTP, allowing the uncoated vesicle to fuse.
Tanigawa, G +5 more
openaire +5 more sources
Cell, 1991 ADP-ribosylation factor (ARF) is an abundant and highly conserved low molecular weight GTP-binding protein that was originally identified as a key element required for the action of cholera toxin in mammalian cells, but whose physiological role is unknown.
T, Serafini +5 more
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COP‐coated vesicles in intracellular protein transport
FEBS Letters, 1995 COP‐coated vesicles have originally been implicated in vesicular transport between subcompartments of the Golgi complex in mammals in a cis to trans direction. More recently, a role for COP‐coated vesicles in transport between the endoplasmic reticulum (ER) and Golgi in mammalian cells has been proposed.
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zeta-COP, a subunit of coatomer, is required for COP-coated vesicle assembly. [PDF]
The Journal of cell biology, 1993 cDNA encoding the 20-kD subunit of coatomer, zeta-COP, predicts a protein of 177-amino acid residues, similar in sequence to AP17 and AP19, subunits of the clathrin adaptor complexes. Polyclonal antibody directed to zeta-COP blocks the binding of coatomer to Golgi membranes and prevents the assembly of COP-coated vesicles on Golgi cisternae.
O, Kuge +7 more
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COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system. [PDF]
The Journal of cell biology, 1994 Rat liver Golgi stacks fragmented when incubated with mitotic but not interphase cytosol in a process dependent on time, temperature, energy (added in the form of ATP) and cdc2 kinase. The cross-sectional length of Golgi stacks fell in the presence of mitotic cytosol by approximately 50% over 30 min without a corresponding decrease in the number of ...
T, Misteli, G, Warren
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Architecture of coatomer: Molecular characterization of delta-COP and protein interactions within the complex [PDF]
, 1996 Copyright © 2011 by The Rockefeller University Press.Coatomer is a cytosolic protein complex that forms the coat of COP I-coated transport vesicles.
Auerbach, S +9 more
core +1 more source
Dissection of GTPase activating proteins reveals functional asymmetry in the COPI coat of budding yeast. [PDF]
, 2019 The Arf GTPase controls formation of the COPI vesicle coat. Recent structural models of COPI revealed the positioning of two Arf1 molecules in contrasting molecular environments.
Arakel, E. +5 more
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The structure of the COPI coat determined within the cell
eLife, 2017 COPI-coated vesicles mediate trafficking within the Golgi apparatus and from the Golgi to the endoplasmic reticulum. The structures of membrane protein coats, including COPI, have been extensively studied with in vitro reconstitution systems using ...
Yury S Bykov +7 more
doaj +1 more source
Three-dimensional architecture and biogenesis of membrane structures associated with hepatitis C virus replication [PDF]
, 2012 All positive strand RNA viruses are known to replicate their genomes in close association with intracellular membranes. In case of the hepatitis C virus (HCV), a member of the family Flaviviridae, infected cells contain accumulations of vesicles forming ...
Antony, Claude +13 more
core +3 more sources