Abstract
Heterotrimeric G proteins have been thought to function on the plasma membrane after activation by transmembrane receptors. Here we show that, after activation by receptors, the G protein betagamma complex selectively translocates to the Golgi. Receptor inactivation results in Gbetagamma translocating back to the plasma membrane. Both translocation processes occur rapidly within seconds. The efficiency of translocation is influenced by the type of gamma subunit present in the G protein. Distinctly different receptor types are capable of inducing the translocation. Receptor-mediated translocation of Gbetagamma can spatially segregate G protein signaling activity.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Bacterial Proteins / metabolism
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CHO Cells
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Cell Membrane / metabolism*
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Cricetinae
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DNA, Complementary / metabolism
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Diffusion
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GTP-Binding Protein beta Subunits / chemistry*
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GTP-Binding Protein beta Subunits / metabolism
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GTP-Binding Protein gamma Subunits / chemistry*
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GTP-Binding Protein gamma Subunits / metabolism
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Genetic Vectors
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Golgi Apparatus / metabolism*
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Green Fluorescent Proteins / metabolism
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Image Processing, Computer-Assisted
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Luminescent Proteins / metabolism
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Microscopy, Fluorescence
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Protein Structure, Tertiary
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Protein Transport
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Signal Transduction
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Time Factors
Substances
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Bacterial Proteins
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Cyan Fluorescent Protein
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DNA, Complementary
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G-protein Beta gamma
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GTP-Binding Protein beta Subunits
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GTP-Binding Protein gamma Subunits
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Luminescent Proteins
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yellow fluorescent protein, Bacteria
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Green Fluorescent Proteins