Phosphoinositide Binding Inhibits Actin Crosslinking and Polymerization by Palladin.

ABSTRACT: Actin cytoskeleton remodeling requires the coordinated action of a large number of actin binding proteins that reorganize the actin cytoskeleton by promoting polymerization, stabilizing filaments, causing branching, or crosslinking filaments. Palladin is a key cytoskeletal actin binding protein whose normal function is to enable cell motility during development of tissues and organs of the embryo and in wound healing, but palladin is also responsible for regulating the ability of cancer cells to become invasive and metastatic. The membrane phosphoinositide phosphatidylinositol (PI) 4,5-bisphosphate [PI(4,5)P₂] is a well-known precursor for intracellular signaling and a bona fide regulator of actin cytoskeleton reorganization. Our results show that two palladin domains [immunoglo

SUBMITTER: Yadav R 

PROVIDER: S-EPMC5525146 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature