Evidence map›Paper›PMID 31409535›Full record

ArticleAdvances in biological regulation2019

The role of phospholipase Cβ on the plasma membrane and in the cytosol: How modular domains enable novel functions.

Suzanne Scarlata

Open access · greenAbstract read
In one paragraph

Article in Advances in biological regulation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

7 citing papers in PubMed, 8 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

Suzanne ScarlataDepartment of Chemistry and Biochemistry, Worcester Polytechnic Institute, 100 Institute Rd., Worcester, MA, 01609, United States. Electronic address: sfscarlata@wpi.edu.
Worcester Polytechnic Institute · US

Funding

Role of caveolae in G protein signalingR01GM116178 · NIGMS · WORCESTER POLYTECHNIC INSTITUTE · PI SCARLATA, SUZANNE F · 2015 to 2018
$1.1M
NIGMS NIH HHS R01 GM116178
6 · The paper itself

Abstract

Phospholipase Cβ (PLCβ) is a signaling enzyme activated by G proteins to generate calcium signals. The catalytic core of PLCβ is surrounded by modular domains that mediate the interaction of the enzyme with known protein partners on the plasma membrane. The C-terminal region PLCβ contains a novel coiled-coil domain that is required for Gαq binding and activation. Recent work has shown that this domain also binds a number of cytosolic proteins that regulate protein translation, and that these proteins compete with Gαq for PLCβ binding. The ability of PLCβ to shuttle between the cytosol to impact protein translation and the plasma membrane to mediate calcium signals puts PLCβ in a central role in cell function.

Indexed as

Calcium SignalingAnimalsCell MembraneCytosolGTP-Binding Protein alpha Subunits, Gq-G11HumansPhospholipase C betaProtein DomainsStructure-Activity RelationshipGNAQ protein, humanGTP-Binding Protein alpha Subunits, Gq-G11Phospholipase C betaG proteinsPhosholipase CProtein domainsTranslational regulation

Identifiers

PMID31409535
PMCPMC6732780
OpenAlexW2966841670

What Socratic 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 Socratic graph.