期刊论文详细信息
FEBS Letters
Role of C‐terminal cytoplasmic domain of the AT2 receptor in ligand binding and signaling
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.
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【 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】

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