| First Author | Qian X | Year | 2009 |
| Journal | Cancer Cell | Volume | 16 |
| Issue | 3 | Pages | 246-58 |
| PubMed ID | 19732724 | Mgi Jnum | J:152691 |
| Mgi Id | MGI:4359534 | Doi | 10.1016/j.ccr.2009.07.031 |
| Citation | Qian X, et al. (2009) The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis. Cancer Cell 16(3):246-58 |
| abstractText | In cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous tensin-3. Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding. |
