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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 beta gamma 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 beta gamma and that it functions constitutively to permit endocytosis.

Citation

H C Lin, J A Duncan, T Kozasa, A G Gilman. Sequestration of the G protein beta gamma subunit complex inhibits receptor-mediated endocytosis. Proceedings of the National Academy of Sciences of the United States of America. 1998 Apr 28;95(9):5057-60

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PMID: 9560227

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