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TitleStructure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly.
Journal, issue, pagesEMBO J, Vol. 29, Issue 3, Page 655-665, Year 2010
Publish dateFeb 3, 2010
AuthorsYi Xing / Till Böcking / Matthias Wolf / Nikolaus Grigorieff / Tomas Kirchhausen / Stephen C Harrison /
PubMed AbstractThe 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 ...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.
External linksEMBO J / PubMed:20033059 / PubMed Central
MethodsEM (single particle)
Resolution15.2 Å
Structure data

EMDB-5118:
Clathrin D6 coat with Hsc70 and Auxilin
Method: EM (single particle) / Resolution: 15.2 Å

Source
  • Bos taurus (cattle)

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