TGF-beta/Smad Signaling

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Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII) and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

1. Massague, J. et al. (2000) Cell 103, 295-309.
2. Caestecker, M.P. et al. (2000) J. Natl. Cancer Inst. 92, 1388-1402.
3. Derynck, R. et al. (2001) Nature Genet. 29, 117-129.
4. Miyazono, K. et al. (2000) Adv. Immunol. 75, 115-157.
5. Derynck, R. et al. (1997) Biochim. Biophys. Acta. 1333, F105-150.
6. López-Casillas, F. et al. (1991) Cell 67, 785-795.
7. Wang, X.F. et al. (1991) Cell 67, 797-805.
8. Derynck, R. et al. (1998) Cell 95, 737-740.
9. Massague, J. et al. (2000) Nat. Rev. Mol. Cell Biol. 1, 169-178.

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TGF-β Receptor I Antibody

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