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Smad2 phosphorylati...
Smad2 phosphorylation by type I receptor : contribution of arginine 462 and cysteine 463 In the C terminus of Smad2 for specificity
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- Yakymovych, Ihor (författare)
- Uppsala universitet,Ludwiginstitutet för cancerforskning
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- Heldin, Carl-Henrik (författare)
- Uppsala universitet,Ludwiginstitutet för cancerforskning
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- Souchelnytskyi, Serhiy (författare)
- Karolinska Institutet,Uppsala universitet,Ludwiginstitutet för cancerforskning
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(creator_code:org_t)
- 2004
- 2004
- Engelska.
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 279:34, s. 35781-35787
- Relaterad länk:
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http://www.ncbi.nlm....
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- 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
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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