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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1998-4-23
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pubmed:databankReference |
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pubmed:abstractText |
Several proteins that contribute to epigenetic mechanisms of gene regulation contain a characteristic motif of unknown function called the SET (Suvar3-9, Enhancer-of-zeste, Trithorax) domain. We have demonstrated that SET domains mediate highly conserved interactions with a specific family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). These include myotubularin, the gene of which is mutated in a subset of patients with X-linked myotubular myopathy, and Sbf1, a newly isolated homologue of myotubularin. In contrast with myotubularin, Sbf1 lacks a functional catalytic domain which dephosphorylates phospho-tyrosine and serine-containing peptides in vitro. Competitive interference of endogenous SET domain-dsPTPase interactions by forced expression of Sbf1 induced oncogenic transformation of NIH 3T3 fibroblasts and impaired the in vitro differentiation of C2 myoblast cells. We conclude that myotubularin-type phosphatases link SET-domain containing components of the epigenetic regulatory machinery with signalling pathways involved in growth and differentiation.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SET protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/myotubularin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1061-4036
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
331-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9537414-3T3 Cells,
pubmed-meshheading:9537414-Amino Acid Sequence,
pubmed-meshheading:9537414-Animals,
pubmed-meshheading:9537414-Binding Sites,
pubmed-meshheading:9537414-Carrier Proteins,
pubmed-meshheading:9537414-Cell Differentiation,
pubmed-meshheading:9537414-Cell Division,
pubmed-meshheading:9537414-Cell Transformation, Neoplastic,
pubmed-meshheading:9537414-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:9537414-Conserved Sequence,
pubmed-meshheading:9537414-Histone Chaperones,
pubmed-meshheading:9537414-Humans,
pubmed-meshheading:9537414-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9537414-Mice,
pubmed-meshheading:9537414-Molecular Sequence Data,
pubmed-meshheading:9537414-Myocardium,
pubmed-meshheading:9537414-Phosphoric Monoester Hydrolases,
pubmed-meshheading:9537414-Protein Binding,
pubmed-meshheading:9537414-Protein Structure, Tertiary,
pubmed-meshheading:9537414-Protein Tyrosine Phosphatases,
pubmed-meshheading:9537414-Protein Tyrosine Phosphatases, Non-Receptor,
pubmed-meshheading:9537414-Proteins,
pubmed-meshheading:9537414-Sequence Homology, Amino Acid,
pubmed-meshheading:9537414-Transcription Factors
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pubmed:year |
1998
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pubmed:articleTitle |
Association of SET domain and myotubularin-related proteins modulates growth control.
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pubmed:affiliation |
Department of Pathology, Stanford University Medical Center, California 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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