Gβγ engages PLCβ3 at multiple sites to reorient and facilitate its activation.
Isaac J Fisher, Kanishka Senarath, Kennedy Outlaw, Kaushik Muralidharan, Elisabeth E Garland-Kuntz, Michelle M Van Camp, Thomas Komay, Leon F Laskowski, Asuka Inoue, Evi Kostenis and 2 more
Article in eLife, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing 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.
Isaac J Fisher *James Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, United States.
Kanishka Senarath *Department of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, United States.
Kennedy OutlawJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, United States.
Kaushik MuralidharanDepartment of Biological Sciences, Purdue University, West Lafayette, United States.
Elisabeth E Garland-KuntzJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, United States.
Michelle M Van CampJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, United States.
Thomas KomayJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, United States.
Leon F LaskowskiJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, United States.
Asuka InoueGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Evi KostenisMolecular, Cellular and Pharmacobiology Section, Institute for Pharmaceutical Biology, University of Bonn, Bonn, Germany.ORCID https://orcid.org/0000-0001-8284-5514
Nevin A LambertDepartment of Pharmacology and Toxicology, Medical College of Georgia, Augusta University, Augusta, United States.ORCID https://orcid.org/0000-0001-7550-0921
Structural Studies of PLCepsilon a regulator of cardiac contractility and hypertrophy.R01HL141076 · NHLBI · PURDUE UNIVERSITY · PI Angeline Marie Lyon · 2018 to 2026
$2.5M
Conventional and unconventional GPCR-G protein couplingR35GM145284 · NIGMS · AUGUSTA UNIVERSITY · PI Nevin Alan Lambert · 2022 to 2026
$1.8M
Mechanisms Underlying Regulation of PLCbeta by heterotrimeric G proteinsR01GM152701 · NIGMS · PURDUE UNIVERSITY · PI Angeline Marie Lyon · 2024 to 2026
$1.1M
Structural Characterization of Gbetagamma-Phospholipase C complexesF32GM145110 · NIGMS · PURDUE UNIVERSITY · PI FISHER, ISAAC · 2022 to 2023
$142k
Deutsche Forschungsgemeinschaft 214362475/GRK1873/3Japan Agency for Medical Research and Development JP22ama121038Japan Agency for Medical Research and Development JP22zf0127007Japan Science and Technology Agency JPMJFR215TJapan Science and Technology Agency JPMJMS2023Japan Society for the Promotion of Science JP24K21281Japan Society for the Promotion of Science JP25H01016National Heart Lung and Blood Institute 1R01HL141076NHLBI NIH HHS R01 HL141076NIGMS NIH HHS 1R01GM152701NIGMS NIH HHS F32 GM145110NIGMS NIH HHS F32GM145110-01NIGMS NIH HHS R01 GM152701NIGMS NIH HHS R35 GM145284NIGMS NIH HHS R35GM145284
6 · The paper itself
Abstract
Phospholipase C β (PLCβ) enzymes are activated by heterotrimeric G protein subunits, increasing hydrolysis of phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) at the plasma membrane. All four human PLCβ isoforms (PLCβ1-4) are activated by Gα
Indexed as
GTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsPhospholipase C betaBinding SitesCell MembraneCryoelectron MicroscopyEnzyme ActivationGTP-Binding Protein alpha Subunits, Gq-G11HumansProtein BindingGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsPhospholipase C betaPLCB3 protein, humanbiochemistrychemical biologyheterotrimeric G proteinhumanlipid signalingmolecular biophysicsphospholipasesignal transductionstructural biology
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.
Gβγ engages PLCβ3 at multiple sites to reorient and facilitate its activation. · full record | OpenQuestion