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).
Schlossman, DM, Schmid, SL, Braell, WA, Rothman, JE
Rapoport, I, Boll, W, Yu, A, Böcking, T, Kirchhausen, T
Böcking, T, Aguet, F, Harrison, SC, Kirchhausen, T
Sousa, R, Lafer, EM
Rothnie, A, Clarke, AR, Kuzmic, P, Cameron, A, Smith, CJ
Xing, Y, Böcking, T, Wolf, M, Grigorieff, N, Kirchhausen, T, Harrison, SC
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