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| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C0237868 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C0036679 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C1366449 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C1539607 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:10644723 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:10644723 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10644723 | pubmed:dateCreated | 2000-2-29 | lld:pubmed |
| pubmed-article:10644723 | pubmed:abstractText | Signal transfer between the protease-activated PAR1 thrombin receptor and membrane-associated heterotrimeric G proteins is mediated by protein-protein interactions. We constructed a yeast signaling system that resolves domain-specific functions of binding from coupling in the Galpha subunit. The endogenous yeast Galpha subunit, Gpa1, does not bind to PAR1 and served as a null structural template. N- and C-terminal portions of mammalian G(i2) and G(16) were substituted back into the Gpa1 template and gain-of-function assessed. The C-terminal third of G(16), but not of G(i2), provides sufficient interactions for coupling to occur with PAR1. The N-terminal two-thirds of G(i2) also contains sufficient determinants to bind and couple to PAR1 and overcome the otherwise negative or missing interactions supplied by the C-terminal third of Gpa1. Replacement of the N-terminal alpha-helix of G(i2), residues 1-34, with those of Gpa1 abolishes coupling but not binding to PAR1 or to betagamma subunits. These data support a model that the N-terminal alphaN helix of the Galpha subunit is physically interposed between PAR1 and the Gbeta subunit and directly assists in transferring the signal between agonist-activated receptor and G protein. | lld:pubmed |
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| pubmed-article:10644723 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10644723 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10644723 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10644723 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10644723 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10644723 | pubmed:author | pubmed-author:SheridanP JPJ | lld:pubmed |
| pubmed-article:10644723 | pubmed:author | pubmed-author:KuliopulosAA | lld:pubmed |
| pubmed-article:10644723 | pubmed:author | pubmed-author:SwiftSS | lld:pubmed |
| pubmed-article:10644723 | pubmed:author | pubmed-author:CovicLL | lld:pubmed |
| pubmed-article:10644723 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10644723 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:10644723 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10644723 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10644723 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10644723 | pubmed:pagination | 2627-35 | lld:pubmed |
| pubmed-article:10644723 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10644723 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10644723 | pubmed:articleTitle | PAR1 thrombin receptor-G protein interactions. Separation of binding and coupling determinants in the galpha subunit. | lld:pubmed |
| pubmed-article:10644723 | pubmed:affiliation | Molecular Cardiology Research Institute, Division of Hematology, New England Medical Center, Boston, Massachusetts 02111, USA. | lld:pubmed |
| pubmed-article:10644723 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10644723 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10644723 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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