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Regulation of cofilin activity by CaMKII and calcineurin
- Source :
- The American journal of the medical sciences. 344(6)
- Publication Year :
- 2012
-
Abstract
- Cofilin promotes actin filament turnover by severing and depolymerizing actin filaments. Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase1 (LIMK1) and is activated when protein phosphatase Slingshot-1L (SSH1L) dephosphorylates this residue. The authors have shown that Ca 2+ -induced cofilin dephosphorylation is mediated by calcineurin (Cn)-dependent activation of SSH1L. In this study, Ca 2+ /calmodulin-dependent protein kinase II (CaMKII) is shown to negatively regulate SSH1L activity and bind to SSH1L in a complex with 14-3-3. Phosphorylation of LIMK1 by CaMKII and its subsequent activation regulates the subcellular localization of SSH1L. Based on these findings, the authors suggest that CaMKII and Cn provide a switch-like mechanism that controls Ca 2+ -dependent LIMK1, SSH1L and cofilin activation, and subsequently actin cytoskeletal reorganization.
- Subjects :
- Cofilin 1
Phosphatase
macromolecular substances
LIMK1
environment and public health
Models, Biological
Dephosphorylation
Ca2+/calmodulin-dependent protein kinase
Phosphoprotein Phosphatases
Serine
Medicine
Humans
Phosphorylation
Actin
Calcimycin
business.industry
Calcineurin
Lim Kinases
General Medicine
Cofilin
Recombinant Proteins
Cell biology
Enzyme Activation
Actin Cytoskeleton
Calcium Ionophores
HEK293 Cells
Biochemistry
14-3-3 Proteins
Gene Knockdown Techniques
MCF-7 Cells
Calcium
business
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Protein Binding
Signal Transduction
Subjects
Details
- ISSN :
- 15382990
- Volume :
- 344
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- The American journal of the medical sciences
- Accession number :
- edsair.doi.dedup.....2d19fbb4ad3de0cfbfba1e66d55ac64b