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Smad2 phosphorylation by type I receptor: contribution of arginine 462 and cysteine 463 In the C terminus of Smad2 for specificity
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
2004 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 279, no 34, 35781-35787 p.Article in journal (Refereed) Published
Abstract [en]

Transforming growth factor-beta (TGFbeta) is a potent regulator of cell proliferation, differentiation, motility, and apoptosis. TGFbeta binds to and activates serine/threonine kinase receptors that phosphorylate Smad2 and Smad3 intracellular signal transducers at two C-terminal serine residues. Here we show that substitutions of Arg-462 and Cys-463 residues, which are in proximity of the C-terminal serine residues, inhibited TGFbeta type I receptor-dependent phosphorylation of the C-terminal Smad2 peptides and full-length GST-Smad2 proteins in vitro. In vivo, mutation of Arg-462 and Cys-463 inhibited TGFbeta1-stimulated phosphorylation of the C-terminal serine residues in Smad2. Moreover, Smad2 with mutated Arg-462 and Cys-463 was less efficient in activation of the Smad2-responsive activin-responsive element-containing luciferase reporter ARE-luc, as compared with the wild-type protein. Thus, Arg-462 and Cys-463, which are in proximity of the C-terminal serine residues, contribute to recognition and phosphorylation of the C terminus of Smad2 by type I TGFbeta receptor.

Place, publisher, year, edition, pages
2004. Vol. 279, no 34, 35781-35787 p.
Keyword [en]
Activin Receptors; Type I/*metabolism, Amino Acid Substitution, Animals, Arginine, Binding Sites, COS Cells, Cercopithecus aethiops, Cysteine, DNA-Binding Proteins/*metabolism, Mice, Mutation, NIH 3T3 Cells, Phosphorylation, Protein Binding, Receptors; Transforming Growth Factor beta/*metabolism, Research Support; Non-U.S. Gov't, Substrate Specificity, Trans-Activators/*metabolism
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-72828DOI: 10.1074/jbc.M404377200PubMedID: 15210694OAI: oai:DiVA.org:uu-72828DiVA: diva2:100739
Available from: 2005-05-30 Created: 2005-05-30 Last updated: 2017-12-14Bibliographically approved

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Yakymovych, IhorHeldin, Carl-HenrikSouchelnytskyi, Serhiy

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