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Vol. 8, Issue 11, 2133-2143, November 1997
Receptors
Thoracic Research Unit and Department of Biochemistry and Molecular
Biology, Mayo Clinic, Rochester, Minnesota 55905
Transforming growth factor 
(TGF) family ligands initiate a
cascade of events capable of modulating cellular growth and differentiation. The receptors responsible for transducing these cellular signals are referred to as the type I and type II TGF receptors. Ligand binding to the type II receptor results in the transphosphorylation and activation of the type I receptor. This heteromeric complex then propagates the signal(s) to downstream effectors. There is presently little data concerning the fate of TGF
receptors after ligand binding, with conflicting reports indicating no
change or decreasing cell surface receptor numbers. To address the fate
of ligand-activated receptors, we have used our previously
characterized chimeric receptors consisting of the ligand binding
domain from the granulocyte/macrophage colony-stimulating factor 
or
receptor fused to the transmembrane and cytoplasmic domain of the
type I or type II TGF receptor. This system not only provides the
necessary sensitivity and specificity to address these types of
questions but also permits the differentiation of endocytic responses
to either homomeric or heteromeric intracellular TGF receptor
oligomerization. Data are presented that show, within minutes of ligand
binding, chimeric TGF receptors are internalized. However, although
all the chimeric receptor combinations show similar internalization
rates, receptor down-regulation occurs only after activation of
heteromeric TGF receptors. These results indicate that effective
receptor down-regulation requires cross-talk between the type I and
type II TGF receptors and that TGF receptor heteromers and
homomers show distinct trafficking behavior.
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