Requirement of membrane-proximal amino acids in the carboxyl-terminal tail for expression of the rat AT1a angiotensin receptor

FEBS Letters
Z GáborikL Hunyady

Abstract

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 (AT1a) 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, [Sar1,Ile8]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 phenylalanine309 and adjacent lysine residues as significant determinants of AT1a receptor expression.

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Citations

May 12, 2004·Molecular and Cellular Endocrinology·László HunyadyKevin J Catt
Sep 1, 2000·Regulatory Peptides·L HunyadyZ Gáborik
Feb 4, 1999·Regulatory Peptides·W G Thomas
Apr 5, 2003·The International Journal of Biochemistry & Cell Biology·Balázs MihalikLászló Hunyady
Oct 20, 2001·Cell Research·D F GuoT Inagami
Mar 1, 2005·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Hiroshi KamimoriMarie-Isabel Aguilar
Jul 12, 2014·Journal of Molecular Endocrinology·Pitchai Balakumar, Gowraganahalli Jagadeesh
Mar 1, 2001·Journal of the Renin-angiotensin-aldosterone System : JRAAS·László HunyadyKevin J Catt
Mar 12, 2010·Molecular Pharmacology·Laura Málaga-DiéguezChristian Nanoff
Nov 1, 2006·Biochimica Et Biophysica Acta·Chunmin DongGuangyu Wu

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