Journal
EMBO JOURNAL
Volume 29, Issue 3, Pages 655-665Publisher
WILEY
DOI: 10.1038/emboj.2009.383
Keywords
chaperone; clathrin-coated vesicle; electron cryomicroscopy; membrane traffic
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Funding
- NIH [GM-36548, GM-62580]
- Human Frontier Science Program Fellowship
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The chaperone Hsc70 drives the clathrin assembly-disassembly cycle forward by stimulating dissociation of a clathrin lattice. A J-domain containing co-chaperone, auxilin, associates with a freshly budded clathrin-coated vesicle, or with an in vitro assembled clathrin coat, and recruits Hsc70 to its specific heavy-chain-binding site. We have determined by electron cryomicroscopy (cryoEM), at about 11 angstrom resolution, the structure of a clathrin coat (in the D6-barrel form) with specifically bound Hsc70 and auxilin. The Hsc70 binds a previously analysed site near the C-terminus of the heavy chain, with a stoichiometry of about one per three-fold vertex. Its binding is accompanied by a distortion of the clathrin lattice, detected by a change in the axial ratio of the D6 barrel. We propose that when Hsc70, recruited to a position close to its target by the auxilin J-domain, splits ATP, it clamps firmly onto its heavy-chain site and locks in place a transient fluctuation. Accumulation of the local strain thus imposed at multiple vertices can then lead to disassembly. The EMBO Journal (2010) 29, 655-665. doi:10.1038/emboj.2009.383; Published online 24 December 2009
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