Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2

Biochem Biophys Res Commun. 2000 May 19;271(3):626-9. doi: 10.1006/bbrc.2000.2671.

Abstract

mDia1 is a downstream effector of Rho small G protein that is implicated in stress fiber formation and cytokinesis. We isolated an mDia1-binding protein and identified it to be IRSp53/BAIAP2. IRSp53 and BAIAP2 have independently been isolated as a 58/53-kDa protein tyrosine phosphorylated in response to insulin and a BAI1-binding protein, respectively. BAI1 is a brain-specific seven-span transmembrane protein capable of inhibiting angiogenesis. The proline-rich formin homology 1 domain of mDia1 bound the Src homology 3 domain of IRSp53/BAIAP2 in a GTP-Rho-dependent manner. The results suggest that IRSp53/BAIAP2 is a downstream effector of mDia1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / metabolism*
  • Cell Line
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Formins
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification
  • Mice
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Protein Binding
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Yeasts
  • rho GTP-Binding Proteins / metabolism*
  • src Homology Domains*

Substances

  • BAIAP2 protein, human
  • Carrier Proteins
  • Diap1 protein, mouse
  • Formins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Recombinant Fusion Proteins
  • rho GTP-Binding Proteins