Abstract
The YIPP (tyrosine-isoleucine-proline-proline, amino acids 319–322) motif within the C-terminal part of the human AT 1 receptor is associated with angiotensin II (AII)-induced activation of the Jak-STAT pathway and phospholipase Cγ1 phosphorylation. We report here that mutations of the YIPP motif strongly affect ligand-binding to the receptor. We analysed AT 1 receptors of the wild type (WT) and 11 mutants with a FLAG-epitope-tag within their C-terminal portion. Mutations of the “P–P” amino acid sequence of this motif decreased both AII binding and the AII-induced intracellular Ca 2+ transients. Mutant and WT receptors were expressed equally in the cell membrane and were localized within the plasma membrane. These results suggest that the “P–P” amino acid sequence within the YIPP motif is important for AII binding to the AT 1 receptor.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
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