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Chatzifrangkeskou, Maria; Yadin, David; Marais, Thibaut; Chardonnet, Solenne; Cohen-Tannoudji, Mathilde; Mougenot, Nathalie; Schmitt, Alain; Crasto, Silvia; Di Pasquale, Elisa; Macquart, Coline; Tanguy, Yannick; Jebeniani, Imen; Pucéat, Michel; Morales Rodriguez, Blanca; Goldmann, Wolfgang H; Dal Ferro, Matteo; Biferi, Maria-Grazia; Knaus, Petra; Bonne, Gisèle; Worman, Howard J; Muchir, Antoine
Human molecular genetics, 09/2018, Letnik: 27, Številka: 17Journal Article
Abstract Hyper-activation of extracellular signal-regulated kinase (ERK) 1/2 contributes to heart dysfunction in cardiomyopathy caused by mutations in the lamin A/C gene (LMNA cardiomyopathy). The mechanism of how this affects cardiac function is unknown. We show that active phosphorylated ERK1/2 directly binds to and catalyzes the phosphorylation of the actin depolymerizing factor cofilin-1 on Thr25. Cofilin-1 becomes active and disassembles actin filaments in a large array of cellular and animal models of LMNA cardiomyopathy. In vivo expression of cofilin-1, phosphorylated on Thr25 by endogenous ERK1/2 signaling, leads to alterations in left ventricular function and cardiac actin. These results demonstrate a novel role for cofilin-1 on actin dynamics in cardiac muscle and provide a rationale on how increased ERK1/2 signaling leads to LMNA cardiomyopathy.
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