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Science 28 May 1993: Vol. 260. no. 5112, pp. 1344 - 1348 DOI: 10.1126/science.8388127
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Articles
Science, Vol 260, Issue 5112, 1344-1348
Copyright © 1993 by American Association for the Advancement of Science
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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- Sorting Nexin 6, a Novel SNX, Interacts with the Transforming Growth Factor-beta Family of Receptor Serine-Threonine Kinases.
- W. T. Parks, D. B. Frank, C. Huff, C. Renfrew Haft, J. Martin, X. Meng, M. P. de Caestecker, J. G. McNally, A. Reddi, S. I. Taylor, et al. (2001)
J. Biol. Chem.
276, 19332-19339
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