Kindlin-2 is required for myocyte elongation and is essential for myogenesis.
Authors Dowling JJ, Vreede AP, Kim S, Golden J, Feldman EL
Submitted By Eva Feldman on 2/23/2009
Status Published
Journal BMC cell biology
Year 2008
Date Published 10/1/2008
Volume : Pages 9 : 36
PubMed Reference 18611274
Abstract 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
Eva FeldmanUniversity of Michigan


Ilkintegrin linked kinase
Fermt2fermitin family homolog 2 (Drosophila)