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Role of the carboxyl‐terminal region, di‐leucine motif and cysteine residues in signalling and internalization of vasopressin V1a receptor
Author(s) -
Preisser Laurence,
Ancellin Nicolas,
Michaelis Lucie,
Cremi Christophe,
Morel Alain,
Corman Bruno
Publication year - 1999
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(99)01360-5
Subject(s) - internalization , receptor , vasopressin receptor , arginine vasopressin receptor 2 , vasopressin , biochemistry , calcium signaling , alanine , hek 293 cells , microbiology and biotechnology , biology , cysteine , amino acid , chemistry , endocrinology , antagonist , enzyme
The structural requirements for internalization and signalling of the vasopressin V1a receptor were investigated in stably transfected HEK‐293 cells. Removal of the 51 C‐terminal amino acids did not affect vasopressin binding, calcium signalling, heterologous desensitization or internalization of the receptor. Deletion of 14 additional amino acids reduced vasopressin‐dependent calcium increase and impaired receptor internalization. Substitution of cysteines 371‐372 did not affect intracellular signalling, but decreased endocytosis by 26%. Substitution of the 361‐362 leucine by alanine residues reduced by 56% V1a receptor sequestration without affecting calcium signalling. These results indicate that di‐cysteine and mostly di‐leucine motifs present in the C‐terminal region of the V1a receptor are involved in its internalization.