CKIP-1 regulates mammalian and zebrafish myoblast fusion

Dominique Baas, Sabine Caussanel-Boude, Alexandre Guiraud, Frederico Calhabeu, Emilie Delaune, Fanny Pilot, Emilie Chopin, Irma Machuca-Gayet, Aurélia Vernay, Stéphanie Bertrand, Jean François Rual, Pierre Jurdic, David E. Hill, Marc Vidal, Laurent Schaeffer, Evelyne Goillot

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23 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)3790-3800
Number of pages11
JournalJournal of Cell Science
Issue number16
Publication statusPublished - 15 Aug 2012
Externally publishedYes


  • Actin cytoskeleton
  • Arp2/3
  • CKIP-1
  • Myoblast fusion
  • Zebrafish muscle development

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