Pan1p: An actin director of endocytosis in yeast

Abstract

The yeast protein Pan1p plays a key role in actin-driven endocytosis. The molecular architecture enables the protein to perform multivalent tasks. First, Pan1p acts as a central scaffold for assembly of coat complex at the endocytic sites through its binding to multiple endocytic proteins. Secondly, Pan1p is also required for normal actin cytoskeleton organization and dynamics at the cell cortex. It is capable of F-actin binding and promoting the Arp2/3-mediated actin nucleation via its WH2 and acid domains. Pan1p, therefore, is responsible for the mechanism of coupling the vesicle coat to actin network in the early steps of internalization. The function of Pan1p is under a negative regulation by the kinase Prk1p. Phosphorylation of Pan1p by Prk1p results in disassembly of the coat complex and dissociation of the vesicle from actin meshwork after internalization. The phosphorylation of Pan1p is possibly reversed by the type 1 phosphatase Glc7p, which will allow Pan1p to be reused for coat assembly in the next round of endocytosis.