CKIP-1 regulates mammalian and zebrafish myoblast fusion
- Authors
- Baas, D., Caussanel-Boude, S., Guiraud, A., Calhabeu, F., Delaune-Henry, E., Pilot, F., Chopin, E., Machuca-Gayet, I., Vernay, A., Bertrand, S., Rual, J.F., Jurdic, P., Hill, D.E., Vidal, M., Schaeffer, L., and Goillot, E.
- ID
- ZDB-PUB-120507-4
- Date
- 2012
- Source
- Journal of Cell Science 125(16): 3790-3800 (Journal)
- Registered Authors
- Baas, Dominique, Bertrand, Stéphanie, Goillot, Evelyne, Schaeffer, Laurent
- Keywords
- none
- MeSH Terms
-
- Actin-Related Protein 2-3 Complex/metabolism
- Animals
- Carrier Proteins/genetics
- Carrier Proteins/metabolism
- Carrier Proteins/physiology*
- Cell Communication/physiology
- Cell Differentiation/physiology
- Cell Fusion
- Cell Line
- Humans
- Intracellular Signaling Peptides and Proteins
- Mammals
- Membrane Fusion/physiology*
- Mice
- Myoblasts/cytology*
- Myoblasts/metabolism
- Transfection
- Zebrafish
- PubMed
- 22553210 Full text @ J. Cell Sci.
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.