Abstract
Signaling from transforming growth factor-β (TGF-β) receptors involves biochemical mechanisms and molecular interactions unique to the transmembrane receptor serinethreonine kinases that bind and transduce signals from ligands belonging to the large family of peptides related to TGF-β (1,2). Members of this family play key roles in regulation of a wide variety of biological end points ranging from early embryonic patterning events to the control of growth, differentiation, and gene expression in adult cells. Although approximately 40 ligands belong to this family, most of the information obtained thus far on signal transduction pathways has come either from genetic studies in Drosophila and Caenorhabditis elegans (3,4) or from study of the pathways activated by a restricted set of ligands expressed in vertebrates, including TGF-β, activin, and the bone morphogenetic proteins, BMPs 2 and 4. Although several pathways, including those involving ras and mitogen-activated protein kinases (MAP-kinases) have been implicated in signaling from TGF-β (2,5), this brief review emphasizes the downstream signaling pathways of these ligands and their receptors attributable to one particular family of signaling intermediates, the recently identified SMAD proteins, which are phosphorylated by the receptor kinases and translocate to the nucleus, where they activate nuclear targets by participating in transcriptional complexes.
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Roberts, A.B., de Caestecker, M.P., Lechleider, R.J. (2000). Signaling from TGF-β Receptors. In: Gutkind, J.S. (eds) Signaling Networks and Cell Cycle Control. Cancer Drug Discovery and Development. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-218-0_3
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DOI: https://doi.org/10.1007/978-1-59259-218-0_3
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