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Volume 272, Number 17, Issue of April 25, 1997 pp. 11444-11451
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Biosynthesis of the Type I and Type II TGF-beta Receptors
IMPLICATIONS FOR COMPLEX FORMATION

(Received for publication, September 12, 1996, and in revised form, January 21, 1997)

Rebecca G. Wells Dagger § , Haya Yankelev Dagger , Herbert Y. Lin Dagger and Harvey F. Lodish Dagger par

From the Dagger  Whitehead Institute, Cambridge, Massachusetts 02142, the § Division of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts 02115, and the par  Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

The TGF-beta type I and type II receptors (Tbeta RI and Tbeta RII) are signaling receptors that form heteromeric cell surface complexes with the TGF-beta s as one of the earliest events in the cellular response to these multifunctional growth factors. Using TGF-beta -responsive mink lung epithelial cells (Mv1Lu), we have determined the half-lives of the endoplasmic reticulum (ER) and mature forms of these receptors. In metabolically labeled cells, approximately 90% of newly synthesized type II receptor undergoes modification of N-linked sugars in the Golgi, with a half-life of 30-35 min; the Golgi-processed form of the receptor has a relatively short metabolic half-life of 2.5 h. In contrast, only 50% of pulse-labeled type I receptor is converted to the Golgi-processed and therefore endoglycosidase H-resistant form, and the endoglycosidase H-sensitive ER form has a half-life of 2.8-3 h. Addition of 100 pM TGF-beta 1 causes the Golgi-processed type II receptor to become less stable, with a half-life of 1.7 h, and also destabilizes the Golgi-processed type I receptor. TGF-beta 1 binding and cross-linking experiments on cells treated with tunicamycin for various times confirm different ER to cell surface processing times for Tbeta RI and Tbeta RII. Our results, which suggest that stable complexes between type I and II TGF-beta receptors do not form until the proteins reach a post-ER compartment (presumably the cell surface), have important implications for our understanding of complex formation and receptor regulation.


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