| First Author | Gao Y | Year | 2000 |
| Journal | J Cell Physiol | Volume | 184 |
| Issue | 3 | Pages | 373-9 |
| PubMed ID | 10911369 | Mgi Jnum | J:63714 |
| Mgi Id | MGI:1861501 | Doi | 10.1002/1097-4652(200009)184:3<373::AID-JCP12>3.0.CO;2-I |
| Citation | Gao Y, et al. (2000) Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration. J Cell Physiol 184(3):373-9 |
| abstractText | Syndecan-4, a member of the syndecan gene family of proteoglycans, is an important regulator of bFGF signaling. In particular, bFGF-dependent regulation of cell growth and migration has been linked to syndecan-4 cytoplasmic domain-mediated interactions. Screening of a yeast two-hybrid library with a cytoplasmic domain of rat syndecan-4 identified a novel binding partner, here termed synectin. Synectin is highly homologous to semaphorin F binding protein semcap1, glucose 1 transporter binding protein glut1cbp, and RGS-GAIP/neuropilin-1 binding protein GIPC. Overexpression of synectin in ECV304 cells in culture led to a dose-dependent inhibition of migration while not affecting cell adhesion or growth rate. We conclude that synectin is involved in syndecan-4-dependent interactions and may play a role in the assembly of syndecan-4 signaling complex. Copyright 2000 Wiley-Liss, Inc. |
