دورية
Cloning and characterization of ATRAP, a novel protein that interacts with the angiotensin II type 1 receptor.
| العنوان: | Cloning and characterization of ATRAP, a novel protein that interacts with the angiotensin II type 1 receptor. |
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| المؤلفون: | Daviet, L, Lehtonen, J Y, Tamura, K, Griese, D P, Horiuchi, M, Dzau, V J |
| المصدر: | Journal of Biological Chemistry; June 1999, Vol. 274 Issue: 24 p17058-62, 5p |
| مستخلص: | The carboxyl-terminal cytoplasmic domain of the angiotensin II type 1 (AT1) receptor has recently been shown to interact with several classes of cytoplasmic proteins that regulate different aspects of AT1 receptor physiology. Employing yeast two-hybrid screening of a mouse kidney cDNA library with the carboxyl-terminal cytoplasmic domain of the murine AT1a receptor as a bait, we have isolated a novel protein with a predicted molecular mass of 18 kDa, which we have named ATRAP (for AT1 receptor-associated protein). ATRAP interacts specifically with the carboxyl-terminal domain of the AT1a receptor but not with those of angiotensin II type 2 (AT2), m3 muscarinic acetylcholine, bradykinin B2, endothelin B, and beta2-adrenergic receptors. The mRNA of ATRAP was abundantly expressed in kidney, heart, and testis but was poorly expressed in lung, liver, spleen, and brain. The ATRAP-AT1a receptor association was confirmed by affinity chromatography, by specific co-immunoprecipitation of the two proteins, and by fluorescence microscopy, showing co-localization of these proteins in intact cells. Overexpression of ATRAP in COS-7 cells caused a marked inhibition of AT1a receptor-mediated activation of phospholipase C without affecting m3 receptor-mediated activation. In conclusion, we have isolated a novel protein that interacts specifically with the carboxyl-terminal cytoplasmic domain of the AT1a receptor and affects AT1a receptor signaling. |
| قاعدة البيانات: | Supplemental Index |
| تدمد: | 00219258 1083351X |
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