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Record W2089237424 · doi:10.1074/jbc.c109.088070

Receptor-regulated Interaction of Activator of G-protein Signaling-4 and Gαi

2010· article· en· W2089237424 on OpenAlexafffund
Şükrü Sadik Öner, Ellen Maher, Billy Breton, Michel Bouvier, J Blumer

Bibliographic record

VenueJournal of Biological Chemistry · 2010
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicProtein Kinase Regulation and GTPase Signaling
Canadian institutionsUniversité de MontréalInstitute for Research in Immunology and Cancer
FundersNational Institute of Neurological Disorders and StrokeNational Institute of General Medical SciencesNational Institute on Drug AbuseCanadian Institutes of Health Research
KeywordsG proteinActivator (genetics)ReceptorAgonistChemistryG protein-coupled receptorCell biologySignal transductionPertussis toxinG beta-gamma complexHeterotrimeric G proteinBiochemistryBiology

Abstract

fetched live from OpenAlex

Activator of G-protein signaling-4 (AGS4), via its three G-protein regulatory motifs, is well positioned to modulate G-protein signal processing by virtue of its ability to bind Gαi-GDP subunits free of Gβγ. Apart from initial observations on the biochemical activity of the G-protein regulatory motifs of AGS4, very little is known about the nature of the AGS4-G-protein interaction, how this interaction is regulated, or where the interaction takes place. As an initial approach to these questions, we evaluated the interaction of AGS4 with Gαi1 in living cells using bioluminescence resonance energy transfer (BRET). AGS4 and Gαi1 reciprocally tagged with either Renilla luciferase (RLuc) or yellow fluorescent protein (YFP) demonstrated saturable, specific BRET signals. BRET signals observed between AGS4-RLuc and Gαi1-YFP were reduced by G-protein-coupled receptor activation, and this agonist-induced reduction in BRET was blocked by pertussis toxin. In addition, specific BRET signals were observed for AGS4-RLuc and α2-adrenergic receptor-Venus, which were Gαi-dependent and reduced by agonist, indicating that AGS4-Gαi complexes are receptor-proximal. These data suggest that AGS4-Gαi complexes directly couple to a G-protein-coupled receptor and may serve as substrates for agonist-induced G-protein activation. Activator of G-protein signaling-4 (AGS4), via its three G-protein regulatory motifs, is well positioned to modulate G-protein signal processing by virtue of its ability to bind Gαi-GDP subunits free of Gβγ. Apart from initial observations on the biochemical activity of the G-protein regulatory motifs of AGS4, very little is known about the nature of the AGS4-G-protein interaction, how this interaction is regulated, or where the interaction takes place. As an initial approach to these questions, we evaluated the interaction of AGS4 with Gαi1 in living cells using bioluminescence resonance energy transfer (BRET). AGS4 and Gαi1 reciprocally tagged with either Renilla luciferase (RLuc) or yellow fluorescent protein (YFP) demonstrated saturable, specific BRET signals. BRET signals observed between AGS4-RLuc and Gαi1-YFP were reduced by G-protein-coupled receptor activation, and this agonist-induced reduction in BRET was blocked by pertussis toxin. In addition, specific BRET signals were observed for AGS4-RLuc and α2-adrenergic receptor-Venus, which were Gαi-dependent and reduced by agonist, indicating that AGS4-Gαi complexes are receptor-proximal. These data suggest that AGS4-Gαi complexes directly couple to a G-protein-coupled receptor and may serve as substrates for agonist-induced G-protein activation.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.002
Threshold uncertainty score0.319

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.014
GPT teacher head0.254
Teacher spread0.240 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations39
Published2010
Admission routes2
Has abstractyes

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