Author:
Baas Dominique,Caussanel-Boude Sabine,Guiraud Alexandre,Calhabeu Frederico,Delaune-Henry Emilie,Pilot Fanny,Chopin Emilie,Machuca-Gayet Irma,Vernay Aurélia,Bertrand Stéphanie,Rual Jean-François,Jurdic Pierre,Hill David E.,Vidal Marc,Schaeffer Laurent,Goillot Evelyne
Abstract
Multinucleated muscle fibres arise by fusion of precursor cells called myoblasts. We previously showed that CKIP-1 ectopic expression in C2C12 myoblasts increased cell fusion. In this work, we report that CKIP-1 depletion drastically impairs C2C12 myoblast fusion in vitro and in vivo during zebrafish muscle development. Within developing fast-twich myotome, Ckip-1 localizes at the periphery of fast precursor cells, closed to the plasma membrane. Unlike wild-type myoblasts that form spatially arrayed multinucleated fast myofibers, Ckip-1 deficient myoblasts show a drastic reduction in fusion capacity. Search for CKIP-1 binding partners identified ARPC1 subunit of Arp2/3 actin nucleation complex essential for myoblast fusion. We demonstrate that CKIP-1, through binding to plasma membrane phosphoinositides via its PH domain, regulates cell morphology and lamellipodia formation by recruiting the Arp2/3 complex at the plasma membrane. These results establish CKIP-1 as a regulator of cortical actin that recruits the Arp2/3 complex at the plasma membrane essential for muscle precursor elongation and fusion.
Publisher
The Company of Biologists
Cited by
25 articles.
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