A yeast DNA J protein required for uncoating of clathrin-coated vesicles in vivo
Clathrin-coated vesicles mediate diverse processes such as nutrient uptake, downregulation of hormone receptors, formation of synaptic vesicles, virus entry, and transport of biosynthetic proteins to lysosomes. Cycles of coat assembly and disassembly are integral features of clathrin-mediated vesicu...
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Published in | Nature cell biology Vol. 2; no. 12; pp. 958 - 963 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Nature Publishing Group
01.12.2000
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Subjects | |
Online Access | Get full text |
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Summary: | Clathrin-coated vesicles mediate diverse processes such as nutrient uptake,
downregulation of hormone receptors, formation of synaptic vesicles, virus
entry, and transport of biosynthetic proteins to lysosomes. Cycles of coat
assembly and disassembly are integral features of clathrin-mediated vesicular
transport (Fig. 1a). Coat assembly involves recruitment
of clathrin triskelia, adaptor complexes and other factors that influence
coat assembly, cargo sequestration, membrane invagination and scission (Fig. 1a). Coat disassembly is thought
to be essential for fusion of vesicles with target membranes and for recycling
components of clathrin coats to the cytoplasm for further rounds of vesicle
formation. In vitro, cytosolic heat-shock protein 70 (Hsp70) and the
J-domain co-chaperone auxilin catalyse coat disassembly. However,
a specific function of these factors in uncoating in vivo has not been
demonstrated, leaving the physiological mechanism and significance of uncoating
unclear. Here we report the identification and characterization of a Saccharomyces
cerevisiae J-domain protein, Aux1. Inactivation of Aux1 results in accumulation
of clathrin-coated vesicles, impaired cargo delivery, and an increased ratio
of vesicle-associated to cytoplasmic clathrin. Our results demonstrate an
in vivo uncoating function of a J domain co-chaperone and establish the
physiological significance of uncoating in transport mediated by clathrin-coated
vesicles. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 1465-7392 1476-4679 1476-4679 |
DOI: | 10.1038/35046619 |