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Kindlin-2 is required for myocyte elongation and is essential for myogenesis.
Dowling JJ, Vreede AP, Kim S, Golden J, Feldman EL
Eva Feldman on 2/23/2009
BMC cell biology
Volume : Pages
9 : 36
BACKGROUND: Integrins are required for normal muscle differentiation and
disruptions in integrin signaling result in human muscle disease. The
intracellular components that regulate integrin function during myogenesis are
poorly understood. Unc-112 is an integrin-associated protein required for muscle
development in C. elegans. To better understand the intracellular effectors of
integrin signaling in muscle, we examined the mammalian homolog of Unc-112,
kindlin-2. RESULTS: Kindlin-2 expression is upregulated during differentiation
and highly enriched at sites of integrin localization. RNAi knockdown of
kindlin-2 in C2C12 cells results in significant abnormalities during the early
stages of myogenesis. Specifically, differentiating myocytes lacking kindlin-2
are unable to elongate and fail to fuse into multinucleated myotubes. These
changes are correlated with decreased cell substratum adhesion and increased
cell motility. They are also associated with redistribution of a known kindlin-2
binding partner, integrin linked kinase (ILK), to the membrane insoluble
subcellular fraction. CONCLUSION: In all, our study reveals kindlin-2 as a novel
integrin adaptor protein important for muscle differentiation, and identifies it
particularly as a critical regulator of myocyte elongation.
Investigators with authorship
University of Michigan
Neuropathy & Neurocognition
integrin linked kinase
fermitin family homolog 2 (Drosophila)
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Please acknowledge all posters, manuscripts or scientific materials that were generated in part or whole using funds from the Diabetic Complications Consortium(DiaComp) using the following text:
Financial support for this work provided by the NIDDK Diabetic Complications Consortium (RRID:SCR_001415, www.diacomp.org), grants DK076169 and DK115255
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