Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase.

Journal Article (Journal Article)

A cDNA encoding the TGF-beta type II receptor protein has been isolated by an expression cloning strategy. The cloned cDNA, when transfected into COS cells, leads to overexpression of an approximately 80 kd protein that specifically binds radioiodinated TGF-beta 1. Excess TGF-beta 1 competes for binding of radioiodinated TGF-beta 1 in a dose-dependent manner and is more effective than TGF-beta 2. The predicted receptor structure includes a cysteine-rich extracellular domain, a single hydrophobic transmembrane domain, and a predicted cytoplasmic serine/threonine kinase domain. A chimeric protein containing the intracellular domain of the type II receptor and expressed in E. coli can phosphorylate itself on serine and threonine residues in vitro, indicating that the cytoplasmic domain of the type II receptor is a functional kinase. This result implicates serine/threonine phosphorylation as an important mechanism of TGF-beta receptor-mediated signaling.

Full Text

Duke Authors

Cited Authors

  • Lin, HY; Wang, XF; Ng-Eaton, E; Weinberg, RA; Lodish, HF

Published Date

  • February 21, 1992

Published In

Volume / Issue

  • 68 / 4

Start / End Page

  • 775 - 785

PubMed ID

  • 1310899

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(92)90152-3


  • eng

Conference Location

  • United States