期刊
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
卷 39, 期 10, 页码 1760-1764出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2006.12.001
关键词
actin; endocytosis; phosphorylation; dephosphorylation; pan1p
The yeast protein Pan1p plays a key role in actin-driven endocytosis. The molecular architecture enables the protein to perform multivalent tasks. First, Pan I p acts as a central scaffold for assembly of coat complex at the endocytic sites through its binding to multiple endocytic proteins. Secondly, Pan I p 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 intemalization. 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 I phosphatase Glc7p, which will allow Pan I p to be reused for coat assembly in the next round of endocytosis. (c) 2006 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据