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J. Biol. Chem., Vol. 268, Issue 30, 22215-22218, 10, 1993
A Moustakas, HY Lin, YI Henis, J Plamondon, MD O'Connor-McCourt and HF Lodish
Transforming growth factors beta (TGF-beta s) are disulfide-linked dimers.
In Rat-1 cells both radioiodinated TGF-beta 1 and -beta 2 bind to and can
be chemically cross-linked to type I and II receptors (which are thought to
mediate effects of cell growth suppression and gene activation), to type
III proteoglycan receptors, and to a novel approximately 50-kDa protein.
After detergent solubilization of cells that were cross-linked with
radioiodinated TGF-beta, antibodies specific for the type II receptor
precipitated labeled receptor types I and III as well as type II. In these
cells, the type III receptor is the predominant TGF-beta-binding protein,
and antibodies specific for it precipitate mainly this cross-linked
receptor. Thus, in the presence of TGF-beta ligand, receptor types II and
III and types II and I form heteromeric complexes. The majority of the type
III receptor does not associate with receptor types I and II, probably
reflecting the relative amounts of the three receptors on the surface of
Rat-1 cells. Since TGF-beta 1 but not TGF-beta 2 binds to the exoplasmic
domain of the type II receptor in the absence of the type III receptor, and
since both TGF-beta 1 and -beta 2 bind with high affinity to the type III
receptor, we suggest that TGF-beta 2, and possibly TGF-beta 1, bind
initially to the type III receptor. The TGF-beta 2-type III receptor
complex would then interact with a type II receptor, thus modulating the
affinity of the type II receptor for TGF-beta 2.
The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142.
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