Auxilin recruits HSPA8:ATP to the clathrin-coated vesicle

Stable Identifier
Reaction [binding]
Homo sapiens
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HSPA8 (also known as HSC70) is recruited to the clathrin-coated vesicle through interaction with DNA J proteins GAK and DNAJC6 (Rapoport et al, 2008; Xing et al, 2010; reviewed in Sousa and Lafer, 2015). Recent studies examining the stoichiometry of uncoating predict between one and three HSPA8 molecules are required per clathrin triskelion for maximal uncoating in vitro (Bocking et al, 2011; Rothnie et al, 2011). After ATP hydrolysis, HSPA8 remains associated with the liberated clathrin, which prevents aberrant repolymerization and association of clathrin (Schlossman et al, 1984; reviewed in Sousa and Lafer, 2015).
Literature References
PubMed ID Title Journal Year
17978091 A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction

Yu, A, Böcking, T, Kirchhausen, T, Boll, W, Rapoport, I

Mol. Biol. Cell 2008
6146630 An enzyme that removes clathrin coats: purification of an uncoating ATPase

Braell, WA, Schlossman, DM, Rothman, JE, Schmid, SL

J. Cell Biol. 1984
21278753 Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating

Böcking, T, Kirchhausen, T, Harrison, SC, Aguet, F

Nat. Struct. Mol. Biol. 2011
26042225 The role of molecular chaperones in clathrin mediated vesicular trafficking

Lafer, EM, Sousa, R

Front Mol Biosci 2015
21482805 A sequential mechanism for clathrin cage disassembly by 70-kDa heat-shock cognate protein (Hsc70) and auxilin

Clarke, AR, Rothnie, A, Cameron, A, Smith, CJ, Kuzmic, P

Proc. Natl. Acad. Sci. U.S.A. 2011
20033059 Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly

Böcking, T, Xing, Y, Kirchhausen, T, Harrison, SC, Wolf, M, Grigorieff, N

EMBO J. 2010
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