ArticleThe Journal of biological chemistry2009
Role of molecular chaperones in G protein beta5/regulator of G protein signaling dimer assembly and G protein betagamma dimer specificity.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Disease-causing mutations in the G protein β5 β-propeller disrupt its chaperonin-mediated folding trajectory.bioRxiv : the preprint server for biology · 2025Article
- Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025Review
- A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle.Nature communications · 2024Article
- Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller.Molecular cell · 2023Article
- Epilepsy in a mouse model of GNB1 encephalopathy arises from altered potassium (GIRK) channel signaling and is alleviated by a GIRK inhibitor.Frontiers in cellular neuroscience · 2023Article
- Novel Binding Partners for CCT and PhLP1 Suggest a Common Folding Mechanism for WD40 Proteins with a 7-Bladed Beta-Propeller Structure.Proteomes · 2021Article
- Oligomerization of A. thaliana Heterotrimeric G Protein Subunits AGB1 and AGG2 In Vitro.The protein journal · 2020Article
- Review
- A novel heat shock protein alpha 8 (Hspa8) molecular network mediating responses to stress- and ethanol-related behaviors.Neurogenetics · 2016Article
- Intermolecular Interaction between Anchoring Subunits Specify Subcellular Targeting and Function of RGS Proteins in Retina ON-Bipolar Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Article
- Comprehensive analysis of heterotrimeric G-protein complex diversity and their interactions with GPCRs in solution.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Retinal cone photoreceptors require phosducin-like protein 1 for G protein complex assembly and signaling.PloS one · 2015Article
- Programmed cell death protein 5 interacts with the cytosolic chaperonin containing tailless complex polypeptide 1 (CCT) to regulate β-tubulin folding.The Journal of biological chemistry · 2014Article
- Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Type 5 G protein beta subunit (Gbeta5) controls the interaction of regulator of G protein signaling 9 (RGS9) with membrane anchors.The Journal of biological chemistry · 2011Article
- The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.Protein science : a publication of the Protein Society · 2011Article
- A conserved protein interaction interface on the type 5 G protein beta subunit controls proteolytic stability and activity of R7 family regulator of G protein signaling proteins.The Journal of biological chemistry · 2010Article
- Proteome changes in platelets activated by arachidonic acid, collagen, and thrombin.Proteome science · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The G protein betagamma subunit dimer (Gbetagamma) and the Gbeta5/regulator of G protein signaling (RGS) dimer play fundamental roles in propagating and regulating G protein pathways, respectively. How these complexes form dimers when the individual subunits are unstable is a question that has remained unaddressed for many years. In the case of Gbetagamma, recent studies have shown that phosducin-like protein 1 (PhLP1) works as a co-chaperone with the cytosolic chaperonin complex (CCT) to fold Gbeta and mediate its interaction with Ggamma. However, it is not known what fraction of the many Gbetagamma combinations is assembled this way or whether chaperones influence the specificity of Gbetagamma dimer formation. Moreover, the mechanism of Gbeta5-RGS assembly has yet to be assessed experimentally. The current study was undertaken to directly address these issues. The data show that PhLP1 plays a vital role in the assembly of Ggamma2 with all four Gbeta1-4 subunits and in the assembly of Gbeta2 with all twelve Ggamma subunits, without affecting the specificity of the Gbetagamma interactions. The results also show that Gbeta5-RGS7 assembly is dependent on CCT and PhLP1, but the apparent mechanism is different from that of Gbetagamma. PhLP1 seems to stabilize the interaction of Gbeta5 with CCT until Gbeta5 is folded, after which it is released to allow Gbeta5 to interact with RGS7. These findings point to a general role for PhLP1 in the assembly of all Gbetagamma combinations and suggest a CCT-dependent mechanism for Gbeta5-RGS7 assembly that utilizes the co-chaperone activity of PhLP1 in a unique way.
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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.