| First Author | Fujiwara T | Year | 2000 |
| Journal | Biochem Biophys Res Commun | Volume | 271 |
| Issue | 3 | Pages | 626-9 |
| PubMed ID | 10814512 | Mgi Jnum | J:62164 |
| Mgi Id | MGI:1858529 | Doi | 10.1006/bbrc.2000.2671 |
| Citation | Fujiwara T, et al. (2000) Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2. Biochem Biophys Res Commun 271(3):626-9 |
| abstractText | 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. Copyright 2000 Academic Press. |
