Evidence map›Paper›PMID 22286107›Full record

ArticleCellular signalling2012

α-Synuclein increases the cellular level of phospholipase Cβ1.

Yuanjian Guo, Barbara Rosati, Suzanne Scarlata

Abstract read
In one paragraph

Article in Cellular signalling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
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  8. Review
  9. Lipid dysfunction and pathogenesis of multiple system atrophy.Acta neuropathologica communications · 2014
    Review
  10. Article
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  12. Article
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

3 authors at 1 institution in 1 country.

Yuanjian GuoDepartment of Physiology & Biophysics, Stony Book University, Stony Brook, NY 11794-8661, USA.
Barbara Rosati
Suzanne Scarlata
Stony Brook University · US

Funding

ACTIVATION OF PHOSPHOLIPASE C BETA BY G PROTEINSR01GM053132 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI SCARLATA, SUZANNE F · 1995 to 2014
$3.5M
NIGMS NIH HHS R01 GM053132PHS HHS NIH053132
6 · The paper itself

Abstract

α-Synuclein is a conserved protein that is a key component in neurodegenerative plaques [1,2]. α-Synuclein binds strongly to phospholipase Cβ (PLCβ) and promotes Ca2+ release in cells. Here, we show that expression of α-synuclein increases the cellular level of PLCβ1 in two neuronal cell lines: PC12 and SK-N-S-SH. The increase in PLCβ1 is not accompanied by changes in the level of RNA or in ubiquitination. Instead, we find that α-synuclein protects PLCβ1 from trypsin digestion and from degradation by the Ca(+2) activated protease calpain. Calpain removes the C-terminal region of the enzyme which mediates activation by Gα(q). We find that in SK-N-SH cells, α-synuclein reduced degradation of PLCβ1 by calpain during Ca2+ signaling allowing the enzyme to remain sensitive to Gα(q) activation. Taken together, our studies show that α-synuclein protects the integrity of PLCβ1 and its ability to be activated by Gα(q), which may in turn impact Ca2+ signaling.

Indexed as

alpha-SynucleinAnimalsCalcimycinCalpainEnzyme ActivatorsHEK293 CellsHumansPC12 CellsPeptide FragmentsPhospholipase C betaProtein BindingProteolysisRatsTranscription, GeneticTrypsinUbiquitinationalpha-SynucleinCalcimycinCalpainEnzyme ActivatorsPeptide FragmentsPhospholipase C betaPLCB1 protein, humanTrypsin

Identifiers

PMID22286107
PMCPMC3288587
OpenAlexW2038401426

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.