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 Scijournal_title
Journal of cell scienceauthors
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 Edoi
10.1242/jcs.101048subject
Has Abstractpub_date
2012-08-15 00:00:00pages
3790-800issue
Pt 16eissn
0021-9533issn
1477-9137pii
jcs.101048journal_volume
125pub_type
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