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Science 28 May 1993:
Vol. 260. no. 5112, pp. 1344 - 1348
DOI: 10.1126/science.8388127

Articles

Science, Vol 260, Issue 5112, 1344-1348
Copyright © 1993 by American Association for the Advancement of Science


articles

Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor

R Ebner, RH Chen, L Shum, S Lawler, TF Zioncheck, A Lee, AR Lopez, and R Derynck

Department of Growth and Development, University of California, San Francisco 94143-0640.

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.


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