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Requirement of membrane‐proximal amino acids in the carboxyl‐terminal tail for expression of the rat AT 1a angiotensin receptor
Author(s) -
Gáborik Zsuzsanna,
Mihalik Balázs,
Jayadev Suman,
Jagadeesh Gowraganahalli,
Catt Kevin J.,
Hunyady László
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00511-0
Subject(s) - angiotensin ii , receptor , alanine , inositol phosphate , mutant , chemistry , angiotensin receptor , amino acid , microbiology and biotechnology , biochemistry , angiotensin ii receptor type 1 , transfection , biology , inositol , gene
A series of deletion mutants was created to analyze the function of the membrane‐proximal region of the cytoplasmic tail of the rat type 1a (AT 1a ) angiotensin receptor. In transiently transfected COS‐7 cells, the truncated mutant receptors showed a progressive decrease in surface expression, with no major change in binding affinity for the peptide antagonist, [Sar 1 ,Ile 8 ]angiotensin II. In parallel with the decrease in receptor expression, a progressive decrease in angiotensin II‐induced inositol phosphate responses was observed. Alanine substitutions in the region 307–311 identified the highly conserved phenylalanine 309 and adjacent lysine residues as significant determinants of AT 1a receptor expression.