RNAi-mediated Hip1R silencing results in stable association between the endocytic machinery and the actin assembly machinery.

ABSTRACT: Actin filaments transiently associate with the endocytic machinery during clathrin-coated vesicle formation. Although several proteins that might mediate or regulate this association have been identified, in vivo demonstration of such an activity has not been achieved. Huntingtin interacting protein 1R (Hip1R) is a candidate cytoskeletal-endocytic linker or regulator because it binds to clathrin and actin. Here, Hip1R levels were lowered by RNA interference (RNAi). Surprisingly, rather than disrupting the transient association between endocytic and cytoskeletal proteins, clathrin-coated structures (CCSs) and their endocytic cargo became stably associated with dynamin, actin, the Arp2/3 complex, and its activator, cortactin. RNAi double-depletion experiments demonstrated that accumulation o

SUBMITTER: Engqvist-Goldstein AE 

PROVIDER: S-EPMC379265 | biostudies-literature | 2004 Apr

REPOSITORIES: biostudies-literature