G‐protein βγ‐binding domains regulate insulin exocytosis in clonal pancreatic β‐cells

FEBS Letters

Zhang, Hui¹  Yasrebi-Nejad, Houri¹  Lang, Jochen¹ 

[1] Division de Biochimie Clinique, Département de Médecine Interne, Centre Médical Universitaire, 1 rue Michel Servet, CH-1211 Geneva 4, Switzerland

关键词: Exocytosis;    Calcium;    Insulin;    G-protein;    Guanosine triphosphate;    GRK2;    G-protein-linked receptor kinase 2;    PH domain;    pleckstrin homology domain;    RGS;    regulator protein of G-protein signalling;    TD;    transducin;    TDα;    the α-subunit of the retinal G-protein transducin;    TM;    transmembrane domain of CD8;    TM-GRK2PH;    the PH domain of the G-protein-linked receptor kinase 2 fused to the transmembrane domain of CD8;   

DOI  :  10.1016/S0014-5793(98)00176-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have tested the putative role of G-protein β-subunits in insulin exocytosis by transient expression of βγ-binding proteins targeted to the plasma membrane. The PH domain of the G-protein-linked receptor kinase 2 fused to the transmembrane domain of a cell surface receptor and the α-subunit of the retinal G-protein transducin inhibited stimulated insulin release from intact and permeabilised HIT-T15 cells. This effect cannot be imputed to an increase in free Gα, as the RGS protein RGS3 did not reverse this effect. Among the isoforms of Gβ examined, Gβ2 was detected on the plasma membrane by confocal immunomicroscopy. These observations suggest a role for G-protein βγ-subunits in insulin exocytosis.

【 授权许可】

Unknown