ArticleThe Journal of cell biology1997
Assembly and intracellular targeting of the betagamma subunits of heterotrimeric G proteins.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- The G protein α chaperone Ric-8 as a potential therapeutic target.Molecular pharmacology · 2015Review
- Ric-8 proteins are molecular chaperones that direct nascent G protein α subunit membrane association.Science signaling · 2011Article
- Adenosine A2A receptor signaling and golf assembly show a specific requirement for the gamma7 subtype in the striatum.The Journal of biological chemistry · 2010Article
- Structural determinants involved in the formation and activation of G protein betagamma dimers.Neuro-Signals · 2009Review
- Assembly and trafficking of heterotrimeric G proteins.Biochemistry · 2007Review
- EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin.Molecular biology of the cell · 2005Article
- Localization of a peripheral membrane protein: Gbetagamma targets Galpha(Z).Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Dual lipid modification of the yeast ggamma subunit Ste18p determines membrane localization of Gbetagamma.Molecular and cellular biology · 1999Article
- Ganglioside structure dictates signal transduction by cholera toxin and association with caveolae-like membrane domains in polarized epithelia.The Journal of cell biology · 1998Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The assembly in living cells of heterotrimeric guanine nucleotide binding proteins from their constituent alpha, beta, and gamma subunits is a complex process, compounded by the multiplicity of the genes that encode them, and the diversity of receptors and effectors with which they interact. Monoclonal anti-beta antibodies (ARC5 and ARC9), raised against immunoaffinity purified beta gamma complexes, recognize beta subunits when not associated with gamma and can thus be used to monitor assembly of beta gamma complexes. Complex formation starts immediately after synthesis and is complete within 30 min. Assembly occurs predominantly in the cytosol, and association of beta gamma complexes with the plasma membrane fraction starts between 15-30 min of chase. Three pools of beta subunits can be distinguished based on their association with gamma subunits, their localization, and their detergent solubility. Association of beta and alpha subunits with detergent-insoluble domains occurs within 1 min of chase, and increases to reach a plateau of near complete detergent resistance within 30 min of chase. Brefeldin A treatment does not interfere with delivery of beta gamma subunits to detergent-insoluble domains, suggesting that assembly of G protein subunits with their receptors occurs distally from the BFA-imposed block of intracellular membrane trafficking and may occur directly at the plasma membrane.
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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.