ArticleThe Journal of biological chemistry2007
A family of G protein βγ subunits translocate reversibly from the plasma membrane to endomembranes on receptor activation.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 101 citations in OpenAlex.
- Reconstitution of Ras-PI3Kγ membrane communication and feedback using light-induced signaling inputs.Nature communications · 2026Article
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- Role of the V2R-βarrestin-Gβγ complex in promoting G protein translocation to endosomes.Communications biology · 2024Article
- Optical control of cell-surface and endomembrane-exclusive β-adrenergic receptor signaling.The Journal of biological chemistry · 2024Article
- Article
- Optical Control of Cell-Surface and Endomembrane-Exclusive β-Adrenergic Receptor Signaling.bioRxiv : the preprint server for biology · 2024Article
- Spatiotemporal Optical Control of Gαq-PLCβ Interactions.ACS synthetic biology · 2024Article
- Beyond the G protein α subunit: investigating the functional impact of other components of the GαiCell communication and signaling : CCS · 2023Article
- PARP1 modulates METTL3 promoter chromatin accessibility and associated LPAR5 RNA mMolecular therapy : the journal of the American Society of Gene Therapy · 2023Article
- CaaX-motif adjacent residues control G protein prenylation under suboptimal conditions.bioRxiv : the preprint server for biology · 2023Article
- Non-canonical Golgi-compartmentalized Gβγ signaling: mechanisms, functions, and therapeutic targets.Trends in pharmacological sciences · 2023Review
- LPAR5 confers radioresistance to cancer cells associated with EMT activation via the ERK/Snail pathway.Journal of translational medicine · 2022Article
- The olfactory receptor OR51E2 activates ERK1/2 through the Golgi-localized Gβγ-PI3Kγ-ARF1 pathway in prostate cancer cells.Frontiers in pharmacology · 2022Article
- Structure of the phosphoinositide 3-kinase (PI3K) p110γ-p101 complex reveals molecular mechanism of GPCR activation.Science advances · 2021Article
- Subtype-dependent regulation of Gβγ signalling.Cellular signalling · 2021Review
- Compartmentalized GPCR Signaling from Intracellular Membranes.The Journal of membrane biology · 2021Review
- Diversity of the Gβγ complexes defines spatial and temporal bias of GPCR signaling.Cell systems · 2021Article
- Live Cell Imaging and Optogenetics-Based Assays for GPCR Activity.Methods in molecular biology (Clifton, N.J.) · 2021Article
- G-protein βγ subunits as multi-functional scaffolds and transducers in G-protein-coupled receptor signaling.Cellular and molecular life sciences : CMLS · 2019Review
- Ligand-induced activation of ERK1/2 signaling by constitutively active GActa pharmacologica Sinica · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The present model of G protein activation by G protein-coupled receptors exclusively localizes their activation and function to the plasma membrane (PM). Observation of the spatiotemporal response of G protein subunits in a living cell to receptor activation showed that 6 of the 12 members of the G protein gamma subunit family translocate specifically from the PM to endomembranes. The gamma subunits translocate as betagamma complexes, whereas the alpha subunit is retained on the PM. Depending on the gamma subunit, translocation occurs predominantly to the Golgi complex or the endoplasmic reticulum. The rate of translocation also varies with the gamma subunit type. Different gamma subunits, thus, confer distinct spatiotemporal properties to translocation. A striking relationship exists between the amino acid sequences of various gamma subunits and their translocation properties. gamma subunits with similar translocation properties are more closely related to each other. Consistent with this relationship, introducing residues conserved in translocating subunits into a non-translocating subunit results in a gain of function. Inhibitors of vesicle-mediated trafficking and palmitoylation suggest that translocation is diffusion-mediated and controlled by acylation similar to the shuttling of G protein subunits (Chisari, M., Saini, D. K., Kalyanaraman, V., and Gautam, N. (2007) J. Biol. Chem. 282, 24092-24098). These results suggest that the continual testing of cytosolic surfaces of cell membranes by G protein subunits facilitates an activated cell surface receptor to direct potentially active G protein betagamma subunits to intracellular membranes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.