p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin

Naoki Watanabe, Pascal Madaule, Tim Reid, Toshimasa Ishizaki, Go Watanabe, Akira Kakizuka, Yuji Saito, Kazuwa Nakao, Brigitte M. Jockusch, Shuh Narumiya

    Research output: Contribution to journalArticlepeer-review

    654 Citations (Scopus)

    Abstract

    Rho small GTPase regulates cell morphology, adhesion; and cytokinesis through the actin cytoskeleton. We have identified a protein, p140mDia, as a downstream effector of Rho. It is a mammalian homolog of Drosophila diaphanous, a protein required for cytokinesis, and belongs to a family of formin-related proteins containing repetitive polyproline stretches. p140mDia binds selectively to the GTP-bound form of Rho and also binds to profilin. p140mDia, profilin and RhoA are co-localized in the spreading lamellae of cultured fibroblasts. They are also co-localized in membrane ruffles of phorbol ester-stimulated sMDCK2 cells, which extend these structures in a Rho-dependent manner. The three proteins are recruited around phagocytic cups induced by fibronectin-coated beads. Their recruitment is not induced after Rho is inactivated by microinjection of botulinum C3 exoenzyme. Overexpression of p140mDia in COS-7 cells induced homogeneous actin filament formation. These results suggest that Rho regulates actin polymerization by targeting profilin via p140mDia beneath the specific plasma membranes.

    Original languageEnglish
    Pages (from-to)3044-3056
    Number of pages13
    JournalEMBO Journal
    Volume16
    Issue number11
    DOIs
    Publication statusPublished - 1997 Jun 2

    Keywords

    • Actin polymerization
    • Diaphanous
    • Membrane ruffle
    • Profilin
    • Rho

    ASJC Scopus subject areas

    • Neuroscience(all)
    • Molecular Biology
    • Biochemistry, Genetics and Molecular Biology(all)
    • Immunology and Microbiology(all)

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