Regulation of cofilin activity by CaMKII and calcineurin.
The American Journal of the Medical Sciences(2012)
摘要
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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关键词
Cofilin activity,Calcium-calmodulin-dependent protein kinase II (CaMKII),Calcineurin (Cn)
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