Regulation of clathrin-mediated endocytosis by dynamic ubiquitination and deubiquitination.

ABSTRACT:

Background

Clathrin-mediated endocytosis in budding yeast requires the regulated recruitment and disassociation of more than 60 proteins at discrete plasma membrane punctae. Posttranslational modifications such as ubiquitination may play important regulatory roles in this highly processive and ordered process. However, although ubiquitination plays an important role in cargo selection, functions for ubiquitination of the endocytic machinery are not known.

Results

We identified the deubiquitinase (DUB) Ubp7 as a late-arriving endocytic protein. Deletion of the DUBs Ubp2 and Ubp7 resulted in elongation of endocytic coat protein lifetimes at the plasma membrane and recruitment of endocytic proteins to internal membranes. These phenotypes could be replicated by expressing a perm

SUBMITTER: Weinberg JS 

PROVIDER: S-EPMC4020423 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature