Evidence map›Paper›PMID 28837400›Full record

ArticleChannels (Austin, Tex.)2017

PKC SUMOylation inhibits the binding of 14-3-3τ to GluK2.

Xiaoling Li, Yan Wang, Aoxue Zhu, Jie Zhou, Yong Li

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Channels (Austin, Tex.), 2017. 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
0.1field-weighted citation impact, top 49% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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 3 institutions in 1 country.

Xiaoling Lia Department of Biochemistry and Molecular Cell Biology , Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine , Shanghai , China.
Yan Wanga Department of Biochemistry and Molecular Cell Biology , Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine , Shanghai , China.
Aoxue Zhua Department of Biochemistry and Molecular Cell Biology , Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine , Shanghai , China.
Jie Zhoua Department of Biochemistry and Molecular Cell Biology , Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine , Shanghai , China.
Yong Lia Department of Biochemistry and Molecular Cell Biology , Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine , Shanghai , China.
Shanghai Jiao Tong University · CNRenji Hospital · CNShanghai First People's Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation and SUMOylation of the kainate receptor (KAR) subunit GluK2 have been shown to regulate KAR surface expression, trafficking and synaptic plasticity. In addition, our previous study has shown that a phosphorylation-dependent interaction of 14-3-3τ and GluK2a-containing receptors contributes to the slow decay kinetics of native KAR-EPSCs. However, it is unknown whether SUMOylation participates in the regulation of the interaction between 14-3-3τ and GluK2a-containing receptors. Here we report that SUMOylation of PKC, but not GluK2, represses the binding of 14-3-3τ to GluK2a via decreasing the phosphorylation level of GluK2a. These results suggest that PKC SUMOylation is an important regulator of the 14-3-3 and GluK2a protein complex and may contribute to regulate the decay kinetics of KAR-EPSCs.

Indexed as

Sumoylation14-3-3 ProteinsBinding SitesCells, CulturedGluK2 Kainate ReceptorHEK293 CellsHumansKainic Acid ReceptorsProtein BindingProtein Kinase C14-3-3 ProteinsGluK2 Kainate ReceptorKainic Acid ReceptorsProtein Kinase C14–3–3τGluK2phosphorylationPKC SUMOylation

Identifiers

PMID28837400
PMCPMC5786187
OpenAlexW2749194376

What OpenQuestion holds

Textmetadata
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.