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rdf:type |
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lifeskim:mentions |
umls-concept:C0015392,
umls-concept:C0017963,
umls-concept:C0033684,
umls-concept:C0040649,
umls-concept:C0178555,
umls-concept:C0332197,
umls-concept:C0456387,
umls-concept:C1292733,
umls-concept:C1321758,
umls-concept:C1414491,
umls-concept:C1704675
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pubmed:issue |
41
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pubmed:dateCreated |
2000-11-13
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pubmed:abstractText |
Yeast two-hybrid techniques were used to identify possible effectors for the heterotrimeric G protein G(z) in human bone marrow cells. Eya2, a human homologue of the Drosophila Eya transcription co-activator, was identified. Eya2 interacts with activated Galpha(z) and at least one other member of the Galpha(i) family, Galpha(i2). Interactions were confirmed in mammalian two-hybrid and glutathione S-transferase fusion protein pull-down assays. Regions of Eya2-mediating interaction were mapped to the C-terminal Eya consensus domain. Eya2 is an intrinsically cytosolic protein that is translocated to the nucleus by members of the Six homeodomain-containing family of proteins. Activated Galpha(z) and Galpha(i2) prevent Eya2 translocation and inhibit Six/Eya2-mediated activation of a reporter gene controlled through the MEF3/TATA promoter. Although G proteins are known to regulate the activity of numerous transcription factors, this regulation is normally achieved indirectly via one or more intermediates. We show here a novel functional regulation of a co-activator directly by G protein subunits.
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pubmed:grant |
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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/EYA2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Eya2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/SIX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SIX4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Six1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32129-34
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10906137-Animals,
pubmed-meshheading:10906137-Bone Marrow Cells,
pubmed-meshheading:10906137-Cell Nucleus,
pubmed-meshheading:10906137-Consensus Sequence,
pubmed-meshheading:10906137-Cytosol,
pubmed-meshheading:10906137-Fluorescent Antibody Technique,
pubmed-meshheading:10906137-GTP-Binding Protein alpha Subunits, Gi-Go,
pubmed-meshheading:10906137-Genes, Reporter,
pubmed-meshheading:10906137-HeLa Cells,
pubmed-meshheading:10906137-Heterotrimeric GTP-Binding Proteins,
pubmed-meshheading:10906137-Homeodomain Proteins,
pubmed-meshheading:10906137-Humans,
pubmed-meshheading:10906137-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10906137-Nerve Tissue Proteins,
pubmed-meshheading:10906137-Nuclear Proteins,
pubmed-meshheading:10906137-Promoter Regions, Genetic,
pubmed-meshheading:10906137-Protein Binding,
pubmed-meshheading:10906137-Protein Subunits,
pubmed-meshheading:10906137-Protein Transport,
pubmed-meshheading:10906137-Protein Tyrosine Phosphatases,
pubmed-meshheading:10906137-Trans-Activators,
pubmed-meshheading:10906137-Two-Hybrid System Techniques
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pubmed:year |
2000
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pubmed:articleTitle |
The alpha subunits of Gz and Gi interact with the eyes absent transcription cofactor Eya2, preventing its interaction with the six class of homeodomain-containing proteins.
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pubmed:affiliation |
Departments of Pharmacology, Medicine and Pathology, and Pediatrics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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