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CKIP-1 regulates mammalian and zebrafish myoblast fusion

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 localises at the periphery of fast precursor cells, closed to the plasma membrane. Unlike wild-type myoblasts that form spatially arrayed multinucleated fast myofibres, Ckip-1-deficient myoblasts show a drastic reduction in fusion capacity. A search for CKIP-1 binding partners identified the 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.
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Submitted on : Wednesday, April 3, 2013 - 4:41:14 PM
Last modification on : Monday, April 25, 2022 - 3:36:02 PM


  • HAL Id : ensl-00807509, version 1


Dominique Baas, Sabine Caussanel-Boude, Alexandre Guiraud, Frederico Calhabeu, Emilie Delaune, et al.. CKIP-1 regulates mammalian and zebrafish myoblast fusion. Journal of Cell Science, Company of Biologists, 2012, 125, pp.3790-3800. ⟨ensl-00807509⟩



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