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ZIRC
ZFIN ID: ZDB-PUB-120507-4
CKIP-1 regulates mammalian and zebrafish myoblast fusion
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.
Date: 2012
Source: Journal of Cell Science 125(16): 3790-3800 (Journal)
Registered Authors: Baas, Dominique, Bertrand, St├ęphanie, 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.
FIGURES
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 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.

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