Auxilin recruits HSPA8:ATP to the clathrin-coated vesicle

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).

HSPA8，亦称HSC70，通过与其结合DNA J蛋白GAK和DNAJC6（参见Rapoport等，2008；Xing等，2010；Sousa和Lafer，2015年综述）而被招募至网格蛋白包被的囊泡中。近期的研究探讨了去包膜过程的化学计量学，预测每个网格蛋白三联体需要一至三个HSPA8分子以实现体外最大程度的去包膜（Bocking等，2011；Rothnie等，2011）。在ATP水解之后，HSPA8依然与释放的网格蛋白相结合，从而防止其异常重新聚合及与网格蛋白的再结合（Schlossman等，1984；参见Sousa和Lafer，2015年综述）。