Receptors and other binding proteins for TGFp

Low numbers of high-affinity receptors for TGFp are found on most normal resting and transformed mammalian cells. Two major receptor species (TGFpRI, 53 kDa, and TGFpRlI, 70-80 kDa) are both serine/threonine kinases. FLach has a small extracellular region, a single transmembrane domain, and an intracytoplasmic serine/threonine kinase domain. Almost all cells, regardless of their origin, express TGFp receptors and bind TGFp with high affinity. Signaling has been shown to require the formation of a trimeric complex consisting of both TGFp receptors I and II and TGFp. Betaglycan (type III receptor) is a third major cell surface protein with high binding affinity to TGFp. Other binding proteins for TGFp include a2-niacroglobulin, fibronectin and p-amyloid precursor.

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