| First Author | Fernández-Larrea J | Year | 1999 |
| Journal | Mol Cell | Volume | 3 |
| Issue | 4 | Pages | 423-33 |
| PubMed ID | 10230395 | Mgi Jnum | J:113805 |
| Mgi Id | MGI:3687686 | Doi | 10.1016/s1097-2765(00)80470-0 |
| Citation | Fernandez-Larrea J, et al. (1999) A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface. Mol Cell 3(4):423-33 |
| abstractText | In general, plasma membrane integral proteins, such as the membrane-anchored growth factor proTGF-alpha, are assumed to be transported to the cell surface via a nonregulated, constitutive pathway. proTGF-alpha C-terminal mutants are retained in an early secretory compartment. Here, using a two-hybrid screen, we identify two TACIPs (proTGF-alpha cytoplasmic domain-interacting proteins) that contain PDZ domains and do not interact with proTGF-alpha C-terminal mutants. The binding specificity of one of them, TACIP18 (previously identified and named Syntenin or mda-9), coincides with that of the component that possibly mediates the normal trafficking of proTGF-alpha. TACIP18 colocalizes and interacts specifically with immature, intracellular forms of proTGF-alpha. Therefore, it appears that the interaction of TACIP18 with proTGF-alpha in the early secretory pathway is necessary for the targeting of the latter to the cell surface. |
