Auxilin recruits HSPA8:ATP to the clathrin-coated vesicle

Stable Identifier
R-HSA-8868660
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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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
6146630 An enzyme that removes clathrin coats: purification of an uncoating ATPase

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

J. Cell Biol. 1984
17978091 A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction

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

Mol. Biol. Cell 2008
21278753 Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating

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

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

Sousa, R, Lafer, EM

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

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

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

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

EMBO J. 2010
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