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pubmed-article:9312122pubmed:abstractTextThe small GTPase Rho is implicated in cytoskeletal rearrangements including stress fiber and focal adhesion formation and in the transcriptional activation of c-fos serum response element. In vitro, Rho-kinase, which is activated by Rho, phosphorylates not only myosin light chain (MLC) (thereby activating myosin ATPase) but also myosin phosphatase, thus inactivating myosin phosphatase. Rho-kinase is involved in the formation of stress fibers and focal adhesions in fibroblasts. Here we show that the expression of constitutively active Rho-kinase increased the level of MLC phosphorylation. The activity of Rho-kinase was necessary for maintaining the vinculin-containing focal adhesions, whereas organized actin stress fibers were not necessary for this. The microinjection of constitutively active Rho-kinase into fibroblasts induced the formation of focal adhesions to some extent under the conditions where organized actin stress fibers were disrupted. The expression of constitutively active Rho-kinase also stimulated the transcriptional activity of c-fos serum response element. These results suggest that Rho-kinase has distinct roles in divergent pathways downstream of Rho, which include MLC phosphorylation leading to stress fiber formation, focal adhesion formation, and gene expression.lld:pubmed
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pubmed-article:9312122pubmed:articleTitleCytoskeletal rearrangements and transcriptional activation of c-fos serum response element by Rho-kinase.lld:pubmed
pubmed-article:9312122pubmed:affiliationDivision of Signal Transduction, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-01, Japan.lld:pubmed
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pubmed-article:9312122pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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