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pubmed-article:11583628pubmed:abstractTextThe type I TGF beta receptor (T beta R-I) is activated by phosphorylation of the GS region, a conserved juxtamembrane segment located just N-terminal to the kinase domain. We have studied the molecular mechanism of receptor activation using a homogeneously tetraphosphorylated form of T beta R-I, prepared using protein semisynthesis. Phosphorylation of the GS region dramatically enhances the specificity of T beta R-I for the critical C-terminal serines of Smad2. In addition, tetraphosphorylated T beta R-I is bound specifically by Smad2 in a phosphorylation-dependent manner and is no longer recognized by the inhibitory protein FKBP12. Thus, phosphorylation activates T beta R-I by switching the GS region from a binding site for an inhibitor into a binding surface for substrate. Our observations suggest that phosphoserine/phosphothreonine-dependent localization is a key feature of the T beta R-I/Smad activation process.lld:pubmed
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pubmed-article:11583628pubmed:articleTitleThe TGF beta receptor activation process: an inhibitor- to substrate-binding switch.lld:pubmed
pubmed-article:11583628pubmed:affiliationLaboratory of Molecular Biophysics, Rockefeller University, New York, NY 10021, USA.lld:pubmed
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pubmed-article:11583628pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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