The βγ subunits of heterotrimeric G proteins acquire detergent insolubility directly at the plasma membrane

FEBS Letters

Rehm, Armin¹  Ploegh, Hidde L.¹ 

[1]Center for Cancer Research, Department of Biology, Massachusetts Institute of Technology, 40 Ames Street, E17-322, Cambridge, MA 02139, USA

关键词: Heterotrimeric G protein βγ subunits;    Monoclonal antibody;    Plasma membrane purification;    Detergent-resistant membrane;    Heptahelical receptor;    Protein kinase C;    G proteins;    heterotrimeric guanine nucleotide binding proteins;    DRM;    detergent-resistant membranes;    TGN;    trans-Golgi network;    ER;    endoplasmic reticulum;    BFA;    brefeldin A;    mAb;    monoclonal antibody;    PNS;    postnuclear supernatant;    TX-100;    Triton X-100;    Staph. A;    Staphylococcus aureus;    WGA;    wheat germ agglutinin;    PMA;    phorbol 12-myristate 13-acetate;    PAF;    platelet-activating factor;   

DOI  :  10.1016/S0014-5793(97)01119-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The subunits of heterotrimeric G proteins, Gα and Gβγ, are found in association with detergent-resistant domains in most mammalian cell types, implicating such domains in G protein-coupled signaling. The pathway by which the βγ complexes are targeted to these detergent-resistant domains was unaffected by the brefeldin A-imposed block on endoplasmic reticulum-to-Golgi transport. We have used subcellular fractionation and β subunit-specific immunoprecipitation to localize the acquisition of detergent insolubility of newly synthesized βγ complexes. The β subunits cofractionate with plasma membranes, and acquire detergent insolubility coincident with arrival in the plasma membrane fractions. This association was not affected by phorbol 12-myristate 13-acetate-induced activation of Proetin kinase C.

【 授权许可】

Unknown