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Exocytic pathway‐independent plasma membrane targeting of heterotrimeric G proteins
Author(s) -
Takida Satoshi,
Wedegaertner Philip B.
Publication year - 2004
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/j.febslet.2004.04.062
Subject(s) - brefeldin a , endoplasmic reticulum , golgi apparatus , microbiology and biotechnology , palmitoylation , heterotrimeric g protein , secretory pathway , transport protein , protein targeting , cytoplasm , chemistry , membrane protein , biology , g protein , signal transduction , biochemistry , membrane , enzyme , cysteine
Heterotrimeric G proteins are lipid‐modified, peripheral membrane proteins that function at the inner surface of the plasma membrane (PM) to relay signals from cell‐surface receptors to downstream effectors. Cellular trafficking pathways that direct nascent G proteins to the PM are poorly defined. In this report, we test the proposal that G proteins utilize the classical exocytic pathway for PM targeting. PM localization of the G protein heterotrimers α s β 1 γ 2 and α q β 1 γ 2 occurred independently of treatment of cells with Brefeldin A, which disrupts the Golgi, or expression of Sar1 mutants, which prevent the formation of endoplasmic reticulum to Golgi transport vesicles. Moreover, the palmitoylation of α q was unaffected by Brefeldin A treatment, even though the palmitoylation of SNAP25 was blocked by Brefeldin A. Non‐palmitoylated mutants of α s and α q failed to stably bind to βγ and displayed a dispersed cytoplasmic localization when co‐expressed with βγ. These findings support a refined model of the PM trafficking pathway of G proteins, involving assembly of the heterotrimer at the endoplasmic reticulum and transport to the PM independently of the Golgi.