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Publication

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
Name Institution Eva Feldman University of Michigan

Complications
All ComplicationsBioinformatics BoneCardiomyopathy CardiovascularGastro-Intestinal (GI) NephropathyNeuropathy & Neurocognition Pediatric Endocrinology Retinopathy UropathyWound Healing

Genes
Symbol Description Ilk integrin linked kinase Fermt2 fermitin family homolog 2 (Drosophila)