Open AccessSequestration of the G protein βγ subunit complex inhibits receptor-mediated endocytosis
Author(s) -
HongCheu Lin,
Joseph A. Duncan,
Tohru Kozasa,
Alfred G. Gilman
Publication year - 1998
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.95.9.5057
Subject(s) - endocytosis , heterotrimeric g protein , microbiology and biotechnology , clathrin , dynamin , receptor mediated endocytosis , cytoskeleton , actin cytoskeleton , biology , protein subunit , actin , g protein , receptor , chemistry , biochemistry , signal transduction , cell , gene
Cell surface receptors that mediate endocytosis cluster into clathrin-coated pits, which pinch off to form vesicles that transport the receptors and their ligands. This multi-step process requires the coordinated action of many factors, including GTP-hydrolyzing proteins such as dynamin and regulators of actin cytoskeleton assembly. We note herein that sequestration of heterotrimeric G protein βγ subunits in intact cells strongly inhibits clathrin-coated pit-mediated endocytosis and causes rearrangement of the actin cytoskeleton. Our results suggest that cells contain a pool of free βγ and that it functions constitutively to permit endocytosis.