AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
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- 1 September 2000
- journal article
- letter
- Published by Springer Nature in Nature
- Vol. 407 (6800) , 94-98
- https://doi.org/10.1038/35024095
Abstract
The vasopressor angiotensin II regulates vascular contractility and blood pressure through binding to type 1 angiotensin II receptors (AT1; refs 1, 2). Bradykinin, a vasodepressor, is a functional antagonist of angiotensin II (ref. 3). The two hormone systems are interconnected by the angiotensin-converting enzyme, which releases angiotensin II from its precursor and inactivates the vasodepressor bradykinin4. Here we show that the AT 1 receptor and the bradykinin (B2) receptor also communicate directly with each other. They form stable heterodimers, causing increased activation of Gαq and Gαi proteins, the two major signalling proteins triggered by AT1. Furthermore, the endocytotic pathway of both receptors changed with heterodimerization. This is the first example of signal enhancement triggered by heterodimerization of two different vasoactive hormone receptors.Keywords
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