| pubmed-article:12748287 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12748287 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:12748287 | lifeskim:mentions | umls-concept:C0752348 | lld:lifeskim |
| pubmed-article:12748287 | lifeskim:mentions | umls-concept:C0751984 | lld:lifeskim |
| pubmed-article:12748287 | lifeskim:mentions | umls-concept:C0205341 | lld:lifeskim |
| pubmed-article:12748287 | lifeskim:mentions | umls-concept:C1135629 | lld:lifeskim |
| pubmed-article:12748287 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:12748287 | pubmed:dateCreated | 2003-5-15 | lld:pubmed |
| pubmed-article:12748287 | pubmed:abstractText | The biological functions of heterotrimeric G proteins and small GTPases are modulated by both extracellular stimuli and intracellular regulatory proteins. Using Saccharomyces cerevisiae two-hybrid screening, we identified tetratricopeptide repeat 1 (TPR1), a 292-amino-acid protein with three TPR motifs, as a Galpha16-binding protein. The interaction was confirmed both in vitro and in transfected mammalian cells, where TPR1 also binds to several other Galpha proteins. TPR1 was found to interact with Ha-Ras preferentially in its active form. Overexpression of TPR1 promotes accumulation of active Ras. TPR1 was found to compete with the Ras-binding domain (RBD) of Raf-1 for binding to the active Ras, suggesting that it may also compete with Ras GTPase-activating protein, thus contributing to the accumulation of GTP-bound Ras. Expression of Galpha16 strongly enhances the interaction between TPR1 and Ras. Removal of the TPR1 N-terminal 112 residues abolishes potentiation by Galpha16 while maintaining the interaction with Galpha16 and the ability to discriminate active Ras from wild-type Ras. We have also observed that LGN, a Galphai-interacting protein with seven TPR motifs, binds Ha-Ras. Thus, TPR1 is a novel adaptor protein for Ras and selected Galpha proteins that may be involved in protein-protein interaction relating to G-protein signaling. | lld:pubmed |
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| pubmed-article:12748287 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12748287 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12748287 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12748287 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12748287 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:12748287 | pubmed:author | pubmed-author:YeRichard DRD | lld:pubmed |
| pubmed-article:12748287 | pubmed:author | pubmed-author:BrowningDarre... | lld:pubmed |
| pubmed-article:12748287 | pubmed:author | pubmed-author:MartyCaroline... | lld:pubmed |
| pubmed-article:12748287 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12748287 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:12748287 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12748287 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12748287 | pubmed:pagination | 3847-58 | lld:pubmed |
| pubmed-article:12748287 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12748287 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12748287 | pubmed:articleTitle | Identification of tetratricopeptide repeat 1 as an adaptor protein that interacts with heterotrimeric G proteins and the small GTPase Ras. | lld:pubmed |
| pubmed-article:12748287 | pubmed:affiliation | Department of Pharmacology, College of Medicine, University of Illinois, Chicago, Illinois 60612, USA. | lld:pubmed |
| pubmed-article:12748287 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12748287 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12748287 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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