Publications [#112871] of G Vann V. Bennett

Papers Published

1. K Kimura, Y Fukata, Y Matsuoka, V Bennett, Y Matsuura, K Okawa, A Iwamatsu, K Kaibuchi, Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase., The Journal of biological chemistry, UNITED STATES, vol. 273 no. 10 (March, 1998), pp. 5542-8, ISSN 0021-9258
   (last updated on 2003/02/18)

   Abstract:
   The small GTPase Rho is believed to regulate the actin cytoskeleton and cell adhesion through its specific targets. We previously identified the Rho targets: protein kinase N, Rho-associated kinase (Rho-kinase), and the myosin-binding subunit (MBS) of myosin phosphatase. Here we purified MBS-interacting proteins, identified them as adducin, and found that MBS specifically interacted with adducin in vitro and in vivo. Adducin is a membrane-skeletal protein that promotes the binding of spectrin to actin filaments and is concentrated at the cell-cell contact sites in epithelial cells. We also found that Rho-kinase phosphorylated alpha-adducin in vitro and in vivo and that the phosphorylation of alpha-adducin by Rho-kinase enhanced the interaction of alpha-adducin with actin filaments in vitro. Myosin phosphatase composed of the catalytic subunit and MBS showed phosphatase activity toward alpha-adducin, which was phosphorylated by Rho-kinase. This phosphatase activity was inhibited by the phosphorylation of MBS by Rho-kinase. These results suggest that Rho-kinase and myosin phosphatase regulate the phosphorylation state of adducin downstream of Rho and that the increased phosphorylation of adducin by Rho-kinase causes the interaction of adducin with actin filaments.

   Keywords:
   Actins • Amino Acid Sequence • Ankyrins • Calmodulin-Binding Proteins • Cell Line • Immunohistochemistry • Intracellular Signaling Peptides and Proteins • Molecular Sequence Data • Myosin-Light-Chain Phosphatase • Phosphopeptides • Phosphoprotein Phosphatase • Phosphorylation • Protein Binding • Protein-Serine-Threonine Kinases • Recombinant Fusion Proteins • analysis • metabolism • metabolism* • physiology