p160(ROCK), a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions

Toshimasa Ishizaki, Mamoru Naito, Kazuko Fujisawa, Midori Maekawa, Naoki Watanabe, Yuji Saito, Shuh Narumiya

    Research output: Contribution to journalArticlepeer-review

    449 Citations (Scopus)

    Abstract

    p160(ROCK) is a serine/threonine protein kinase that binds selectively to GTP-Rho and is activated by this binding. To identify its function, we transfected HeLa cells with wild type and mutants of p160(ROCK) and examined morphology of the transfected cells. Transfection with wild type and mutants containing the kinase domain and the coiled-coil forming region induced focal adhesions and stress fibers, while no induction was observed with a kinase-defective mutant or a mutant containing only the kinase domain. Furthermore, Rho-induced formation of focal adhesions and stress fibers was inhibited by co-expression of a mutant defective in both kinase and Rho-binding activities. Rho, however, still induced an increase in F-actin content in these cells. These results suggest that p160(ROCK) works downstream of Rho to induce formation of focal adhesions and that Rho-induced actin polymerization is mediated by other effector(s).

    Original languageEnglish
    Pages (from-to)118-124
    Number of pages7
    JournalFEBS Letters
    Volume404
    Issue number2-3
    DOIs
    Publication statusPublished - 1997 Mar 10

    Keywords

    • Actin polymerization
    • Focal adhesion
    • Rho
    • Stress fiber
    • p160(ROCK)

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology

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