Role of C‐terminal cytoplasmic domain of the AT2 receptor in ligand binding and signaling

FEBS Letters

Gray, Amanda¹  Pulakat, Lakshmidevi¹  Burns, Veronica¹  Johnson, Janean¹  Gavini, Nara¹  Knowle, Dieter¹ 

[1] Department of Biological Sciences, Bowling Green State University, Bowling Green, OH 43403, USA

关键词: Angiotensin II;    AT2 receptor;    C-terminal cytoplasmic tail;    cGMP;    ErbB3;    Xenopus oocyte;   

DOI  :  10.1016/S0014-5793(02)03005-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A stop codon at position 322 was introduced to generate a truncated, C-terminal-deleted AT2 receptor. Expression studies in Xenopus oocytes showed that C-terminal-deleted AT2 had reduced affinity to [¹²⁵I]angiotensin II (K _d=1.7 nM) and enhanced binding of the AT2-specific peptidic ligand [¹²⁵I]CGP42112A (K _d=0.097 nM). AT2 activation by angiotensin II resulted in reduction of cGMP levels in oocytes and this reduction was further enhanced by C-terminal deletion, implying that the C-terminus may have a negative effect on the AT2-mediated cGMP reduction. Moreover, interaction of the AT2 with the ATP-binding domain of the human ErbB3 receptor in yeast two-hybrid assay was abolished by C-terminal deletion. In summary, the C-terminal cytoplasmic tail of AT2 modulates its ligand binding and signaling properties.

【 授权许可】

Unknown