Role of Auxilin and Heat Shock Protein 70kDa in Clathrin Uncoating
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چکیده
منابع مشابه
4SCIENTIFIC REVIEW Role of Auxilin and Heat Shock Protein 70kDa in Clathrin Uncoating
An interaction between auxilin and heat shock protein 70kDa (Hsc70) was initially discovered in 1995. There exists a large amount of data supporting the basis for their interaction in vitro and their function in clathrin uncoating in vivo. This review examines the key experiments in elucidating this interaction and introduces a third protein that may connect constriction or fission with hsc70/a...
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The DnaJ protein auxilin has been extensively studied in vitro as a cofactor for uncoating clathrin-coated vesicles by the chaperone Hsc70. Recent studies provide the first evidence that auxilin plays this role in vivo, and work on a new mammalian auxilin suggests the protein may have more complex cellular functions.
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We have examined the roles of Hsc70 and auxilin in the uncoating of clathrin-coated vesicles (CCVs) during neuronal endocytosis. We identified two peptides that inhibit the ability of Hsc70 and auxilin to uncoat CCVs in vitro. When injected into nerve terminals, these peptides inhibited both synaptic transmission and CCV uncoating. Mutation of a conserved HPD motif within the J domain of auxili...
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An essential stage in endocytic coated vesicle recycling is the dissociation of clathrin from the vesicle coat by the molecular chaperone, 70-kDa heat-shock cognate protein (Hsc70), and the J-domain-containing protein, auxilin, in an ATP-dependent process. We present a detailed mechanistic analysis of clathrin disassembly catalyzed by Hsc70 and auxilin, using loss of perpendicular light scatter...
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ژورنال
عنوان ژورنال: Einstein Journal of Biology and Medicine
سال: 2016
ISSN: 1559-5498,1559-5501
DOI: 10.23861/ejbm20052197