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TitleClathrin-coat disassembly illuminates the mechanisms of Hsp70 force generation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 23, Issue 9, Page 821-829, Year 2016
Publish dateAug 1, 2016
AuthorsRui Sousa / Hsien-Shun Liao / Jorge Cuéllar / Suping Jin / José M Valpuesta / Albert J Jin / Eileen M Lafer /
PubMed AbstractHsp70s 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 linksNat Struct Mol Biol / PubMed:27478930 / PubMed Central
MethodsEM (single particle)
Resolution28.0 Å
Structure data

EMDB-3442:
Cryo-EM reconstructions of clathrin D6 cages
Method: EM (single particle) / Resolution: 28.0 Å

EMDB-4035:
Cryo-EM reconstruction of clathrin D6 cages + full length Hsc70
Method: EM (single particle) / Resolution: 28.0 Å

EMDB-4036:
Cryo-EM reconstruction of clathrin D6 cages + Hsc70 Delta C
Method: EM (single particle) / Resolution: 28.0 Å

Source
  • Mus musculus (house mouse)
  • Bos taurus (cattle)
  • Rattus norvegicus (Norway rat)

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