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Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin


Slingshot (SSH) phosphatases and LIM kinases (LIMK) regulate actin dynamics via a reversible phosphorylation (inactivation) of serine 3 in actin-depolymerizing factor (ADF) and cofilin. Here we demonstrate that a multi-protein complex consisting of SSH-1L, LIMK1, actin, and the scaffolding protein, 14-3-3zeta, is involved, along with the kinase, PAK4, in the regulation of ADF/cofilin activity. Endogenous LIMK1 and SSH-1L interact in vitro and co-localize in vivo, and this interaction results in dephosphorylation and downregulation of LIMK1 activity. We also show that the phosphatase activity of purified SSH-1L is F-actin dependent and is negatively regulated via phosphorylation by PAK4. 14-3-3zeta binds to phosphorylated slingshot, decreases the amount of slingshot that co-sediments with F-actin, but does not alter slingshot activity. Here we define a novel ADF/cofilin phosphoregulatory complex and suggest a new mechanism for the regulation of ADF/cofilin activity in mediating changes to the actin cytoskeleton.

Type Journal
ISBN 0261-4189 (Print)
Authors Soosairajah, J.;Maiti, S.;Wiggan, O.;Sarmiere, P.;Moussi, N.;Sarcevic, B.;Sampath, R.;Bamburg, J. R.;Bernard, O. :
Publisher Name EMBO JOURNAL
Published Date 2005-01-01
Published Volume 24
Published Issue 3
Published Pages 473-86
Status Published in-print
URL link to publisher's version