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Am J Physiol Heart Circ Physiol 278: H1736-H1743, 2000;
0363-6135/00 $5.00
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Vol. 278, Issue 6, H1736-H1743, June 2000

beta 1-Integrin and PI 3-kinase regulate RhoA-dependent activation of skeletal alpha -actin promoter in myoblasts

Lei Wei, Wei Zhou, Lu Wang, and Robert J. Schwartz

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030

RhoA GTPase, a regulator of actin cytoskeleton, is also involved in regulating c-fos gene expression through its effect on serum response factor (SRF) transcriptional activity. We have also shown that RhoA plays a critical role in myogenesis and regulates expression of SRF-dependent muscle genes, including skeletal alpha -actin. In the present study, we examined whether the RhoA signaling pathway cross talks with other myogenic signaling pathways to modulate skeletal alpha -actin promoter activity in myoblasts. We found that extracellular matrix proteins and the beta 1-integrin stimulated RhoA-dependent activation of the alpha -actin promoter. The muscle-specific isoform beta 1D selectively activated the alpha -actin promoter in concert with RhoA but inhibited the c-fos promoter. In addition, focal adhesion kinase (FAK) and phosphatidylinositol (PI) 3-kinase were required for full activation of the alpha -actin promoter by RhoA. Expression of a dominant negative mutant of FAK, application of wortmannin to cultured myoblasts, or expression of a dominant negative mutant of PI 3-kinase inhibited alpha -actin promoter activity induced by RhoA. These results suggest that RhoA, beta 1-integrin, FAK, and PI 3-kinase serve together as an important signaling network in regulating muscle gene expression.

RhoA signaling; beta 1D-integrin; focal adhesion kinase


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