9346908

Source:http://linkedlifedata.com/resource/pubmed/id/9346908

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0031715, umls-concept:C0037083, umls-concept:C0439855, umls-concept:C1334468, umls-concept:C1514873, umls-concept:C1522492, umls-concept:C1546857, umls-concept:C1556066, umls-concept:C1619636, umls-concept:C1710082
pubmed:issue	44
pubmed:dateCreated	1997-12-9
pubmed:abstractText	Mothers against Dpp-related or Smad proteins are essential components of serine/threonine kinase receptor signaling pathways that are regulated by phosphorylation. Recently, it was demonstrated that Smad2 interacts transiently with and is a direct substrate of the transforming growth factor-beta (TGF-beta) type I receptor, TbetaRI. Phosphorylation sites on Smad2 were localized to a carboxyl-terminal fragment containing three serine residues at positions 464, 465, and 467. In this report, we show that TbetaRI specifically phosphorylates Smad2 on serines 465 and 467. Serine 464 is not a site of phosphorylation, but is important for efficient phosphorylation of Smad2. Phosphorylation at both sites is required to mediate association of Smad2 with Smad4 in mammalian cells, while in yeast, Smad2 interacts directly with Smad4 and does not require phosphorylation. Mutation of either serine residue 465 or 467 prevents dissociation of Smad2 from activated TbetaRI and blocks TGF-beta-dependent signaling and Smad2 transcriptional activity. These results indicate that receptor-dependent phosphorylation of Smad2 on serines 465 and 467 is required in mammalian cells to permit association with Smad4 and to propagate TGF-beta signals.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Activin Receptors, Type I, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth..., http://linkedlifedata.com/resource/pubmed/chemical/SMAD2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SMAD4 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Smad2 Protein, http://linkedlifedata.com/resource/pubmed/chemical/Smad4 Protein, http://linkedlifedata.com/resource/pubmed/chemical/TGF-beta type I receptor, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
pubmed:status	MEDLINE
pubmed:month	Oct
pubmed:issn	0021-9258
pubmed:author	pubmed-author:AbdollahSS, pubmed-author:AttisanoLL, pubmed-author:HayashiHH, pubmed-author:Macías-SilvaMM, pubmed-author:TsukazakiTT, pubmed-author:WranaJ LJL
pubmed:issnType	Print
pubmed:day	31
pubmed:volume	272
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	27678-85
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:9346908-Activin Receptors, Type I, pubmed-meshheading:9346908-Cell Line, pubmed-meshheading:9346908-DNA-Binding Proteins, pubmed-meshheading:9346908-Humans, pubmed-meshheading:9346908-Phosphorylation, pubmed-meshheading:9346908-Protein-Serine-Threonine Kinases, pubmed-meshheading:9346908-Receptors, Transforming Growth Factor beta, pubmed-meshheading:9346908-Serine, pubmed-meshheading:9346908-Signal Transduction, pubmed-meshheading:9346908-Smad2 Protein, pubmed-meshheading:9346908-Smad4 Protein, pubmed-meshheading:9346908-Trans-Activators
pubmed:year	1997
pubmed:articleTitle	TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling.
pubmed:affiliation	Program in Developmental Biology and Division of Gastroenterology, The Hospital for Sick Children, Toronto, Ontario, Canada, M5G 1X8.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't