Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly

@article{Xing2010StructureOC,
  title={Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly},
  author={Yi Xing and Till B{\"o}cking and Matthias Wolf and Nikolaus Grigorieff and Tomas Kirchhausen and Stephen C Harrison},
  journal={The EMBO Journal},
  year={2010},
  volume={29},
  pages={655 - 665}
}
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… CONTINUE READING
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