| Title: | "Apm4, the mu subunit of yeast AP-2 interacts with Pkc1, and mutation of the Pkc1 consensus phosphorylation site Thr176 inhibits AP-2 recruitment to endocytic sites" |
| Address: | "Department of Biomedical Science; University of Sheffield; Sheffield, UK" |
| ISSN/ISBN: | 1942-0889 (Print) 1942-0889 (Electronic) 1942-0889 (Linking) |
| Abstract: | "The AP-2 endocytic adaptor has been extensively characterized in mammalian cells and is considered to play a role both in cargo binding and in formation of endocytic sites. However, despite our detailed knowledge of mechanistic aspects of endocytic complex assembly and disassembly in the model organism Saccharomyces cerevisiae, no function of AP-2 had been described in wild-type yeast under normal growth conditions. A recent study however revealed that disruption of the complex caused by deletion of the gene encoding its mu subunit (APM4) caused defects in cell polarity such that responses to pheromone, nutritional status and cell wall damage were affected. Furthermore, a homozygous deletion of the mu subunit gene in Candida albicans affected its ability to grow hyphae. Direct binding to the yeast cell wall stress sensor Mid2 was detected, and in an apm4 deletion strain Mid2 showed reduced re-localization to the mother bud neck region following cell wall damage with calcofluor or to the mating projection tip. Here we demonstrate an interaction between Apm4 and the yeast cell wall integrity pathway component Pkc1 and show that mutation of the predicted Pkc1 site in the Apm4 hinge region affects recruitment of the AP-2 complex to endocytic sites" |
| Keywords: | Saccharomyces cerevisiae adaptor proteins endocytosis phosphorylation protein kinase C; |
| Notes: | "PubMed-not-MEDLINEChapa-Y-Lazo, Bernardo Ayscough, Kathryn R eng G0601600/MRC_/Medical Research Council/United Kingdom 2014/10/28 Commun Integr Biol. 2014 Apr 2; 7:e28522. doi: 10.4161/cib.28522. eCollection 2014" |
