@article {6340,
	title = {Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly.},
	journal = {The EMBO Journal},
	volume = {29},
	year = {2010},
	month = {2010 Feb 3},
	pages = {655-65},
	abstract = {<p>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 A 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.</p>
},
	keywords = {Animals, Auxilins, Biological, Cattle, Clathrin, Clathrin-Coated Vesicles, Cryoelectron Microscopy, HSC70 Heat-Shock Proteins, Models, Molecular, Multiprotein Complexes, Protein Binding, Protein Multimerization, Protein Structure, Quaternary, Secondary},
	issn = {1460-2075},
	doi = {10.1038/emboj.2009.383},
	author = {Xing, Yi and B{\"o}cking, Till and Wolf, Matthias and Grigorieff, Nikolaus and Kirchhausen, Tomas and Harrison, Stephen C}
}
