pubmed-article:11375483 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11375483 | lifeskim:mentions | umls-concept:C1519661 | lld:lifeskim |
pubmed-article:11375483 | pubmed:issue | 5524 | lld:pubmed |
pubmed-article:11375483 | pubmed:dateCreated | 2001-6-15 | lld:pubmed |
pubmed-article:11375483 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:abstractText | Dysfunction of the tubby protein results in maturity-onset obesity in mice. Tubby has been implicated as a transcription regulator, but details of the molecular mechanism underlying its function remain unclear. Here we show that tubby functions in signal transduction from heterotrimeric GTP-binding protein (G protein)-coupled receptors. Tubby localizes to the plasma membrane by binding phosphatidylinositol 4,5-bisphosphate through its carboxyl terminal "tubby domain." X-ray crystallography reveals the atomic-level basis of this interaction and implicates tubby domains as phosphorylated-phosphatidyl- inositol binding factors. Receptor-mediated activation of G protein alphaq (Galphaq) releases tubby from the plasma membrane through the action of phospholipase C-beta, triggering translocation of tubby to the cell nucleus. The localization of tubby-like protein 3 (TULP3) is similarly regulated. These data suggest that tubby proteins function as membrane-bound transcription regulators that translocate to the nucleus in response to phosphoinositide hydrolysis, providing a direct link between G-protein signaling and the regulation of gene expression. | lld:pubmed |
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pubmed-article:11375483 | pubmed:language | eng | lld:pubmed |
pubmed-article:11375483 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11375483 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11375483 | pubmed:month | Jun | lld:pubmed |
pubmed-article:11375483 | pubmed:issn | 0036-8075 | lld:pubmed |
pubmed-article:11375483 | pubmed:author | pubmed-author:ShawW LWL | lld:pubmed |
pubmed-article:11375483 | pubmed:author | pubmed-author:ShapiroLL | lld:pubmed |
pubmed-article:11375483 | pubmed:author | pubmed-author:GomezC ACA | lld:pubmed |
pubmed-article:11375483 | pubmed:author | pubmed-author:ZhaoJJ | lld:pubmed |
pubmed-article:11375483 | pubmed:author | pubmed-author:MyszkaD GDG | lld:pubmed |
pubmed-article:11375483 | pubmed:author | pubmed-author:BairdC LCL | lld:pubmed |
pubmed-article:11375483 | pubmed:author | pubmed-author:BoggonT JTJ | lld:pubmed |
pubmed-article:11375483 | pubmed:author | pubmed-author:SantagataSS | lld:pubmed |
pubmed-article:11375483 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11375483 | pubmed:day | 15 | lld:pubmed |
pubmed-article:11375483 | pubmed:volume | 292 | lld:pubmed |
pubmed-article:11375483 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11375483 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11375483 | pubmed:pagination | 2041-50 | lld:pubmed |
pubmed-article:11375483 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:11375483 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11375483 | pubmed:articleTitle | G-protein signaling through tubby proteins. | lld:pubmed |
pubmed-article:11375483 | pubmed:affiliation | Ruttenberg Cancer Center, Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine of New York University, 1425 Madison Avenue New York, NY 10029, USA. | lld:pubmed |
pubmed-article:11375483 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11375483 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:11375483 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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