Role of the carboxyl‐terminal region, di‐leucine motif and cysteine residues in signalling and internalization of vasopressin V1a receptor

FEBS Letters

Creminon, Christophe²  Preisser, Laurence¹  Corman, Bruno¹  Michaelis, Lucie¹  Ancellin, Nicolas¹  Morel, Alain³ 

[1] Service de Biologie Cellulaire, CEA/Saclay, Gif-sur-Yvette 91191, Cedex, France;Service de Physiologie et Pharmacologie, CEA/Saclay, Gif-sur-Yvette 91191, Cedex, France;Université d'Angers, Angers, France

关键词: Vasopressin;    V1a receptor;    Internalization;    Di-leucine motif;    C-terminal region;    Calcium signalling;   

DOI  :  10.1016/S0014-5793(99)01360-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown