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• W1970534551 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 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." @default.
• W1970534551 created "2016-06-24" @default.
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• W1970534551 date "2012-12-01" @default.
• W1970534551 modified "2023-10-17" @default.
• W1970534551 title "Regulation of Cofilin Activity by CaMKII and Calcineurin" @default.
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• W1970534551 doi "https://doi.org/10.1097/maj.0b013e318244745b" @default.
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