期刊
AMERICAN JOURNAL OF THE MEDICAL SCIENCES
卷 344, 期 6, 页码 462-472出版社
ELSEVIER SCIENCE INC
DOI: 10.1097/MAJ.0b013e318244745b
关键词
Cofilin activity; Calcium-calmodulin-dependent protein kinase II (CaMKII); Calcineurin (Cn)
资金
- Jilin Provincial Science & Technology Department [20080723]
- NSFC [81172000, 30772488]
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 Ca2+-induced cofilin dephosphorylation is mediated by calcineurin (Cn)-dependent activation of SSH1L. In this study, Ca2+/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 Ca2+-dependent LIMK1, SSH1L and cofilin activation, and subsequently actin cytoskeletal reorganization.
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