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| Title | Clathrin-coat disassembly illuminates the mechanisms of Hsp70 force generation. |
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| Journal, issue, pages | Nat Struct Mol Biol, Vol. 23, Issue 9, Page 821-829, Year 2016 |
| Publish date | Aug 1, 2016 |
 Authors | Rui Sousa / Hsien-Shun Liao / Jorge Cuéllar / Suping Jin / José M Valpuesta / Albert J Jin / Eileen M Lafer /   |
| PubMed Abstract | Hsp70s use ATP hydrolysis to disrupt protein-protein associations and to move macromolecules. One example is the Hsc70- mediated disassembly of the clathrin coats that form on vesicles during ...Hsp70s use ATP hydrolysis to disrupt protein-protein associations and to move macromolecules. One example is the Hsc70- mediated disassembly of the clathrin coats that form on vesicles during endocytosis. Here, we exploited the exceptional features of these coats to test three models-Brownian ratchet, power-stroke and entropic pulling-proposed to explain how Hsp70s transform their substrates. Our data rule out the ratchet and power-stroke models and instead support a collision-pressure mechanism whereby collisions between clathrin-coat walls and Hsc70s drive coats apart. Collision pressure is the complement to the pulling force described in the entropic pulling model. We also found that self-association augments collision pressure, thereby allowing disassembly of clathrin lattices that have been predicted to be resistant to disassembly. These results illuminate how Hsp70s generate the forces that transform their substrates. |
 External links | Nat Struct Mol Biol / PubMed:27478930 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 28.0 Å |
| Structure data |  EMDB-3442:  EMDB-4035:  EMDB-4036: |
| Source |
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Mus musculus (house mouse)
