Medical College of Wisconsin
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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

Date

05/18/2000

Pubmed ID

10814512

DOI

10.1006/bbrc.2000.2671

Scopus ID

2-s2.0-0034685631 (requires institutional sign-in at Scopus site)   72 Citations

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.

Author List

Fujiwara T, Mammoto A, Kim Y, Takai Y

Author

Akiko Mammoto MD, PhD Associate Professor in the Pediatrics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Carrier Proteins
Cell Line
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Membrane Proteins
Mice
Nerve Tissue Proteins
Protein Binding
Recombinant Fusion Proteins
Yeasts
rho GTP-Binding Proteins
src Homology Domains