RGD Reference Report - Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin. - Rat Genome Database

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

Authors: Soosairajah, J  Maiti, S  Wiggan, O  Sarmiere, P  Moussi, N  Sarcevic, B  Sampath, R  Bamburg, JR  Bernard, O 
Citation: Soosairajah J, etal., EMBO J. 2005 Feb 9;24(3):473-86. Epub 2005 Jan 20.
RGD ID: 11535125
Pubmed: PMID:15660133   (View Abstract at PubMed)
PMCID: PMC548651   (View Article at PubMed Central)
DOI: DOI:10.1038/sj.emboj.7600543   (Journal Full-text)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Ssh1Ratgrowth cone  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Ssh1  (slingshot protein phosphatase 1)


Additional Information