ArticleProceedings of the National Academy of Sciences of the United States of America2012
G-protein signaling leverages subunit-dependent membrane affinity to differentially control βγ translocation to intracellular membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 40 citations in OpenAlex.
- Spatiotemporal Optical Control of Gαq-PLCβ Interactions.ACS synthetic biology · 2024Article
- Molecular annotation of G protein variants in a neurological disorder.Cell reports · 2023Article
- Beyond the G protein α subunit: investigating the functional impact of other components of the GαiCell communication and signaling : CCS · 2023Article
- CaaX-motif adjacent residues control G protein prenylation under suboptimal conditions.bioRxiv : the preprint server for biology · 2023Article
- Gβγ signaling regulates microtubule-dependent control of Golgi integrity.Cellular signalling · 2023Article
- Structural Basis of the Interaction of the G Proteins, GαiBiomedicines · 2023Article
- Non-canonical Golgi-compartmentalized Gβγ signaling: mechanisms, functions, and therapeutic targets.Trends in pharmacological sciences · 2023Review
- Molecular regulation of PLCβ signaling.Methods in enzymology · 2023Review
- Genetically encoded tools for in vivo G-protein-coupled receptor agonist detection at cellular resolution.Clinical and translational medicine · 2022Review
- A model for how Gβγ couples Gα to GPCR.The Journal of general physiology · 2022Article
- The olfactory receptor OR51E2 activates ERK1/2 through the Golgi-localized Gβγ-PI3Kγ-ARF1 pathway in prostate cancer cells.Frontiers in pharmacology · 2022Article
- A short C-terminal peptide in Gγ regulates Gβγ signaling efficacy.Molecular biology of the cell · 2021Article
- Article
- Subtype-dependent regulation of Gβγ signalling.Cellular signalling · 2021Review
- Deep Learning-Enabled Label-Free On-Chip Detection and Selective Extraction of Cell Aggregate-Laden Hydrogel Microcapsules.Small (Weinheim an der Bergstrasse, Germany) · 2021Article
- Diversity of the Gβγ complexes defines spatial and temporal bias of GPCR signaling.Cell systems · 2021Article
- Blue light-triggered photochemistry and cytotoxicity of retinal.Cellular signalling · 2020Article
- G-protein βγ subunits as multi-functional scaffolds and transducers in G-protein-coupled receptor signaling.Cellular and molecular life sciences : CMLS · 2019Review
- Article
- Optical approaches for single-cell and subcellular analysis of GPCR-G protein signaling.Analytical and bioanalytical chemistry · 2019Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Activation of G-protein heterotrimers by receptors at the plasma membrane stimulates βγ-complex dissociation from the α-subunit and translocation to internal membranes. This intermembrane movement of lipid-modified proteins is a fundamental but poorly understood feature of cell signaling. The differential translocation of G-protein βγ-subunit types provides a valuable experimental model to examine the movement of signaling proteins between membranes in a living cell. We used live cell imaging, mathematical modeling, and in vitro measurements of lipidated fluorescent peptide dissociation from vesicles to determine the mechanistic basis of the intermembrane movement and identify the interactions responsible for differential translocation kinetics in this family of evolutionarily conserved proteins. We found that the reversible translocation is mediated by the limited affinity of the βγ-subunits for membranes. The differential kinetics of the βγ-subunit types are determined by variations among a set of basic and hydrophobic residues in the γ-subunit types. G-protein signaling thus leverages the wide variation in membrane dissociation rates among different γ-subunit types to differentially control βγ-translocation kinetics in response to receptor activation. The conservation of primary structures of γ-subunits across mammalian species suggests that there can be evolutionary selection for primary structures that confer specific membrane-binding affinities and consequent rates of intermembrane movement.
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Registered trials
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.