Evidence map›Paper›PMID 33901492›Full record

ArticleThe Journal of biological chemistry

Dissociation of the G protein βγ from the Gq-PLCβ complex partially attenuates PIP2 hydrolysis.

Dinesh Kankanamge, Sithurandi Ubeysinghe, Mithila Tennakoon, Priyanka Devi Pantula, Kishalay Mitra, Lopamudra Giri, Ajith Karunarathne

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed.

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  8. An integrated mechanism of GProceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Dinesh KankanamgeDepartment of Chemistry and Biochemistry, The University of Toledo, Toledo, Ohio, USA.
Sithurandi UbeysingheDepartment of Chemistry and Biochemistry, The University of Toledo, Toledo, Ohio, USA.
Mithila TennakoonDepartment of Chemistry and Biochemistry, The University of Toledo, Toledo, Ohio, USA.
Priyanka Devi PantulaDepartment of Chemical Engineering, Indian Institute of Technology, Hyderabad, Sangareddy, Telangana, India.
Kishalay MitraDepartment of Chemical Engineering, Indian Institute of Technology, Hyderabad, Sangareddy, Telangana, India.
Lopamudra GiriDepartment of Chemical Engineering, Indian Institute of Technology, Hyderabad, Sangareddy, Telangana, India.
Ajith KarunarathneDepartment of Chemistry and Biochemistry, The University of Toledo, Toledo, Ohio, USA. Electronic address: Ajith.karunarathne@utoledo.edu.

Funding

Diverse membrane affinities of Gγ members deferentially modulate the Gβγ effectors and cell behaviorsR15GM126455 · NIGMS · UNIVERSITY OF TOLEDO · PI KARUNARATHNE, WELIVITIYA KANKANAMLAGE AJITH · 2018 to 2018
$441k
NIGMS NIH HHS R15 GM126455
6 · The paper itself

Abstract

Phospholipase C β (PLCβ), which is activated by the Gq family of heterotrimeric G proteins, hydrolyzes the inner membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2), generating diacylglycerol and inositol 1,4,5-triphosphate (IP3). Because Gq and PLCβ regulate many crucial cellular processes and have been identified as major disease drivers, activation and termination of PLCβ signaling by the Gαq subunit have been extensively studied. Gq-coupled receptor activation induces intense and transient PIP2 hydrolysis, which subsequently recovers to a low-intensity steady-state equilibrium. However, the molecular underpinnings of this equilibrium remain unclear. Here, we explored the influence of signaling crosstalk between Gq and Gi/o pathways on PIP2 metabolism in living cells using single-cell and optogenetic approaches to spatially and temporally constrain signaling. Our data suggest that the Gβγ complex is a component of the highly efficient lipase Gαq

Indexed as

Cell MembraneGTP-Binding Protein alpha Subunits, Gq-G11HeLa CellsHumansHydrolysisModels, MolecularPhosphatidylinositol 4,5-DiphosphatePhospholipase C betaProtein BindingProtein ConformationSignal TransductionGTP-Binding Protein alpha Subunits, Gq-G11Phosphatidylinositol 4,5-DiphosphatePhospholipase C betaadaptationGPCRGαq(GTP)opsinsOptogeneticsPIP2 recoveryPLCβsignal transductionsteady-state

Identifiers

PMID33901492
PMCPMC8138763

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.