Expression cloning and characterization of the TGF-beta type III receptor.


Journal Article

The rat TGF-beta type III receptor cDNA has been cloned by overexpression in COS cells. The encoded receptor is an 853 amino acid protein with a large N-terminal extracellular domain containing at least one site for glycosaminoglycan addition, a single hydrophobic transmembrane domain, and a 41 amino acid cytoplasmic tail with no obvious signaling motif. Introduction of the cDNA into COS cells and L6 myoblasts induces expression of a heterogenously glycosylated 280-330 kd protein characteristic of the type III receptor that binds TGF-beta 1 specifically. In L6 myoblasts lacking the endogenous type III receptor, expression of the recombinant receptor leads to an increase in the amount of ligand bound and cross-linked to surface type II TGF-beta receptors. This indicates that the type III receptor may regulate the ligand-binding ability or surface expression of the type II receptor.

Full Text

Duke Authors

Cited Authors

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

Published Date

  • November 15, 1991

Published In

Volume / Issue

  • 67 / 4

Start / End Page

  • 797 - 805

PubMed ID

  • 1657407

Pubmed Central ID

  • 1657407

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(91)90074-9


  • eng

Conference Location

  • United States