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(TGF-) Receptors Define a
Model System for Investigating the Role of Homomeric and Heteromeric
Receptors in TGF- Signaling
(Received for publication, April 10, 1996, and in revised form, June 7, 1996)
From the Thoracic Research Unit and Department of Biochemistry and
Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905
Transforming growth factor-
(TGF-) belongs
to a family of ligands that regulate cell growth and differentiation.
The most commonly observed receptors are referred to as the type I,
type II, and type III (betaglycan) TGF- receptors. Two receptor
models have been presented to account for the various cellular
responses to TGF-. The first proposes that all TGF- signaling
results from the formation of a heteromeric type I/type II complex,
while the second suggests that distinct type I or type II TGF-
receptor combinations mediate aspects of TGF- signaling. We have
addressed this general question relating to TGF- signaling by
constructing chimeric receptors consisting of the extracellular domain
of the granulocyte/macrophage colony-stimulating factor (GM-CSF) 
or
receptor fused to the transmembrane and cytoplasmic domain of the
type I or type II TGF- receptor. Since high affinity GM-CSF binding
requires dimerization of the and ligand binding subunits, the
response elicited by defined type I and/or type II TGF- receptor
cytoplasmic domain homomers or heteromers can be examined. We show in
mesenchymal AKR-2B cells that while TGF--dependent
transient luciferase activity, endogenous gene activity, and long-term
biological responses are similarly induced by activating the
chimeric heteromeric receptors with GM-CSF as the endogenous TGF-
receptor, chimeric homomeric type I/type I or type II/type II
receptors are signaling-incompetent.
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