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.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Baas D,Caussanel-Boude S,Guiraud A,Calhabeu F,Delaune E,Pilot F,Chopin E,Machuca-Gayet I,Vernay A,Bertrand S,Rual JF,Jurdic P,Hill DE,Vidal M,Schaeffer L,Goillot E

doi

10.1242/jcs.101048

subject

Has Abstract

pub_date

2012-08-15 00:00:00

pages

3790-800

issue

Pt 16

eissn

0021-9533

issn

1477-9137

pii

jcs.101048

journal_volume

125

pub_type

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