|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
2001-10-3
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
The 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.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Activin Receptors, Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
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/RAD53 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Smad2 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/TGF-beta type I receptor,
http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus Binding Protein 1A,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
1097-2765
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
8
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
671-82
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:11583628-Activin Receptors, Type I,
pubmed-meshheading:11583628-Amino Acid Sequence,
pubmed-meshheading:11583628-Cell Cycle Proteins,
pubmed-meshheading:11583628-Crystallography, X-Ray,
pubmed-meshheading:11583628-DNA-Binding Proteins,
pubmed-meshheading:11583628-Immunoblotting,
pubmed-meshheading:11583628-Models, Biological,
pubmed-meshheading:11583628-Models, Molecular,
pubmed-meshheading:11583628-Molecular Sequence Data,
pubmed-meshheading:11583628-Molecular Structure,
pubmed-meshheading:11583628-Phosphorylation,
pubmed-meshheading:11583628-Protein Binding,
pubmed-meshheading:11583628-Protein Structure, Secondary,
pubmed-meshheading:11583628-Protein Structure, Tertiary,
pubmed-meshheading:11583628-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11583628-Receptors, Transforming Growth Factor beta,
pubmed-meshheading:11583628-Recombinant Fusion Proteins,
pubmed-meshheading:11583628-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11583628-Smad2 Protein,
pubmed-meshheading:11583628-Tacrolimus Binding Protein 1A,
pubmed-meshheading:11583628-Trans-Activators,
pubmed-meshheading:11583628-Transforming Growth Factor beta
|
|
pubmed:year |
2001
|
|
pubmed:articleTitle |
The TGF beta receptor activation process: an inhibitor- to substrate-binding switch.
|
|
pubmed:affiliation |
Laboratory of Molecular Biophysics, Rockefeller University, New York, NY 10021, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
