Literature DB >> 8388127

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

R Ebner1, R H Chen, L Shum, S Lawler, T F Zioncheck, A Lee, A R Lopez, R Derynck.   

Abstract

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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Year:  1993        PMID： 8388127     DOI： 10.1126/science.8388127

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  65 in total

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