An expanded V2 receptor retention signal

FEBS Letters

Le Gouill, Christian¹  Innamorati, Giulio¹  Birnbaumer, Mariel¹ 

[1]Department of Anesthesiology, UCLA School of Medicine, Los Angeles, CA 90095, USA

关键词: V2 receptor;    Phosphorylation;    Recycling;    Dephosphorylation;    Retention motif;    Arrestin;    hV2R;    human type 2 vasopressin receptor;    GRK;    G protein-coupled receptor kinase;   

DOI  :  10.1016/S0014-5793(02)03709-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Following ligand-promoted internalization the human type 2 vasopressin receptor (hV2R) is not recycled to the cell surface after removal of the agonist. A retention motif consisting of a serine triplet present in the cytoplasmic tail was previously found to require for retention, but serine 357, and threonines 359, 360 located upstream were not examined. Evidence is now presented that substitution of these amino acids did not change V2 internalization although it reduced the levels of arginine vasopressin (AVP)-induced phosphorylation as compared to the wild type (WT). Contrary to the WT hV2R, these mutant receptors were recycled to the cell surface after a 2 h incubation in the absence of AVP identifying these changed residues as additional members of the retention motif of the hV2R.

【 授权许可】

Unknown