Journal
TRAFFIC
Volume 7, Issue 12, Pages 1596-1603Publisher
BLACKWELL PUBLISHING
DOI: 10.1111/j.1600-0854.2006.00497.x
Keywords
chaperone; clathrin; coated vesicles; Hsc70; Hsp70; motor protein; protein import
Categories
Funding
- NIGMS NIH HHS [GM52522, R01 GM052522] Funding Source: Medline
- NINDS NIH HHS [NS29051, R56 NS029051, R01 NS029051] Funding Source: Medline
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Hsp70s are ubiquitous chaperones that use ATP hydrolysis to drive a variety of protein processing reactions, including a number of steps in protein trafficking. Recent studies have shed light on how ATP might generate conformational changes in an Hsp70 molecule and how such changes might be harnessed to drive processes as diverse as protein import into subcellular organelles and uncoating of clathrin-coated vesicles.
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