| First Author | Ebner R | Year | 1993 |
| Journal | Science | Volume | 260 |
| Issue | 5112 | Pages | 1344-8 |
| PubMed ID | 8388127 | Mgi Jnum | J:25557 |
| Mgi Id | MGI:73273 | Doi | 10.1126/science.8388127 |
| Citation | Ebner R, et al. (1993) Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor. Science 260(5112):1344-8 |
| abstractText | Transforming growth factor-beta (TGF-beta) affects cellular proliferation, differentiation, and interaction with the extracellular matrix primarily through interaction with the type I and type II TGF-beta receptors. The type II receptors for TGF-beta and activin contain putative serine-threonine kinase domains. A murine serine-threonine kinase receptor, Tsk 7L, was cloned that shared a conserved extracellular domain with the type II TGF-beta receptor. Overexpression of Tsk 7L alone did not increase cell surface binding of TGF-beta, but coexpression with the type II TGF-beta receptor caused TGF-beta to bind to Tsk 7L, which had the size of the type I TGF-beta receptor. Overexpression of Tsk 7L inhibited binding of TGF-beta to the type II receptor in a dominant negative fashion. Combinatorial interactions and stoichiometric ratios between the type I and II receptors may therefore determine the extent of TGF-beta binding and the resulting biological activities. |
