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Articles in PresS, published online ahead of print October 23, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00370.2002
Submitted on August 15, 2002
Accepted on October 17, 2002
1 Bichemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia
* To whom correspondence should be addressed. E-mail: christina.mitchell.edu.au.
The skeletal muscle LIM protein 1, SLIM1, is highly expressed in skeletal and cardiac muscle and its expression is significantly downregulated in dilated human cardiomyopathy. However, the function of SLIM1 is unknown. In this study, we investigated the intracellular localization of SLIM1. Endogenous and recombinant SLIM1 localized to the nucleus, stress fibres and focal adhesions in skeletal myoblasts plated on fibronectin, collagen, or laminin. However, following inhibition of integrin signaling either by plating on poly-L-lysine, or by soluble RGD peptide, SLIM1 localized diffusely in the cytosol, with decreased nuclear expression. Disruption of the actin cytoskeleton by cytochalasin D, did not inhibit nuclear localization of SLIM1 in integrin-activated cells. Green fluorescent protein-tagged SLIM1 shuttled into the nucleus of untransfected NIH-3T3 cells, in a heterokaryon fusion assay. Overexpression of SLIM1 in Sol8 myoblasts inhibited cell adhesion and promoted cell spreading and migration. These studies show SLIM1 localizes in an integrin-dependent manner to the nucleus and focal adhesions where it functions downstream of integrin activation to promote cell spreading and migration.
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