Evidence map›Paper›PMID 23377541›Full record

ArticleNature structural & molecular biology2013

Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain.

Angeline M Lyon, Somnath Dutta, Cassandra A Boguth, Georgios Skiniotis, John J G Tesmer

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.6field-weighted citation impact, top 7% of its field
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

63 citing papers in PubMed, 106 citations in OpenAlex.

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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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  17. The mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2023
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3 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Angeline M LyonLife Sciences Institute, University of Michigan, Ann Arbor, Michigan, USA.
Somnath Dutta
Cassandra A Boguth
Georgios Skiniotis
John J G Tesmer
University of Michigan–Ann Arbor · US

Funding

XenograftP30CA046592 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alexey I Nesvizhskii · 1988 to 2026
$178.2M
PUBLIC HEALTH DEMONSTRATIONP60DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1985 to 2012
$26.5M
Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
Structure, function, and inhibition of G protein-coupled receptor kinasesR01HL071818 · NHLBI · UNIVERSITY OF TEXAS AUSTIN · PI TESMER, JOHN · 2004 to 2023
$7.1M
Structural Studies of Galphaq and Its Complexes at the Cell MembraneR01HL086865 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESMER, JOHN · 2007 to 2015
$3.0M
Architectural Basis of Leptin Transmembrane SignalingR01DK090165 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SKINIOTIS, GEORGIOS · 2011 to 2017
$2.3M
SFG Investigation of Peptide and Protein Orientations in MembranesR01GM081655 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHEN, ZHAN · 2008 to 2012
$1.5M
NCI NIH HHS P30 CA046592NCI NIH HHS Y1-CO-1020NHLBI NIH HHS HL071818NHLBI NIH HHS HL086865,NHLBI NIH HHS R01 HL071818NHLBI NIH HHS R01 HL086865NIDDK NIH HHS DK090165NIDDK NIH HHS DK20572.NIDDK NIH HHS P30 DK020572NIDDK NIH HHS P60 DK020572NIDDK NIH HHS R01 DK090165NIGMS NIH HHS GM081655NIGMS NIH HHS R01 GM081655NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

Phospholipase C-β (PLCβ) is directly activated by Gαq, but the molecular basis for how its distal C-terminal domain (CTD) contributes to maximal activity is poorly understood. Herein we present both the crystal structure and cryo-EM three-dimensional reconstructions of human full-length PLCβ3 in complex with mouse Gαq. The distal CTD forms an extended monomeric helical bundle consisting of three antiparallel segments with structural similarity to membrane-binding bin-amphiphysin-Rvs (BAR) domains. Sequence conservation of the distal CTD suggests putative membrane and protein interaction sites, the latter of which bind the N-terminal helix of Gαq in both the crystal structure and cryo-EM reconstructions. Functional analysis suggests that the distal CTD has roles in membrane targeting and in optimizing the orientation of the catalytic core at the membrane for maximal rates of lipid hydrolysis.

Indexed as

AnimalsCatalytic DomainCryoelectron MicroscopyCrystallography, X-RayGTP-Binding Protein alpha Subunits, Gq-G11HumansMiceModels, MolecularPhospholipase C betaProtein ConformationProtein Structure, TertiaryGTP-Binding Protein alpha Subunits, Gq-G11Phospholipase C betaPLCB3 protein, human

Identifiers

PMID23377541
PMCPMC3594540
OpenAlexW2080854025

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.