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Receptor Kinase Complexes
(Received for publication, November 8, 1994)
Transforming growth factor-
(TGF-) signaling in Mv1Lu
lung epithelial cells requires coexpression of TGF- receptors I
(TR-I) and II (TR-II), two distantly related transmembrane
serine/threonine kinases that form a heteromeric complex upon ligand
binding. Here, we examine the formation of TGF- receptor
homooligomers and their possible contribution to signaling. TR-I
can contact ligand bound to TR-II, but not ligand free in the
medium, and thus cannot form ligandinduced homo-oligomers. TR-II,
which binds ligand on its own, formed oligomeric complexes when
overexpressed in transfected COS cells. However, these complexes were
largely ligand-independent and involved immature receptor protein.
Since ligand-induced homo-oligomers could not be obtained with the
wild-type TGF- receptors, we studied receptor cytoplasmic domain
homo-oligomerization by using receptor chimeras. The extracellular
domain of TR-II was fused to the transmembrane and cytoplasmic
domains of TR-I, yielding TR-II/I, and the extracellular
domain of TR-I was fused to the transmembrane and cytoplasmic
domains of TR-II, yielding TR-I/II. When cotransfected with
wild-type receptors and exposed to ligand, TR-II/I formed a
complex with TR-I, and TR-I/II formed a complex with
TR-II, thus yielding complexes with homologous cytoplasmic
domains. TR-II/I transfected alone or with TR-I did not
restore TGF- responsiveness in TR-II-defective cell mutants.
Furthermore, TR-II/I acted in a dominant negative fashion,
inhibiting restoration of TGF- responsiveness by a cotransfected
TR-II in TR-II-defective cells and by a cotransfected
TR-I in TR-I-defective cells. Similarly, TR-I/II
transfected alone or with TR-II did not restore TGF-
responsiveness and acted in a dominant negative fashion against
TR-I. Together with previous genetic and biochemical evidence,
these results suggest that TGF- mediates transcriptional and
antiproliferative responses through the heteromeric
TR-I
TR-II complex and not through homo-oligomeric
TR-I or TR-II complexes.
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