Evidence map›Paper›PMID 28827787›Full record

ArticleScientific reports2017

Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells.

Murat R Gainullin, Ilya Yu Zhukov, Xiaoying Zhou, Yingxi Mo, Lidiia Astakhova, Ingemar Ernberg, Liudmila Matskova

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Cofilin(s) and Mitochondria: Function Beyond Actin Dynamics.International journal of molecular sciences · 2025
    Review
  3. E3 ubiquitin ligases in nasopharyngeal carcinoma and implications for therapies.Journal of molecular medicine (Berlin, Germany) · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Cofilin-2 Acts as a Marker for Predicting Radiotherapy Response and Is a Potential Therapeutic Target in Nasopharyngeal Carcinoma.Medical science monitor : international medical journal of experimental and clinical research · 2018
    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

7 authors at 5 institutions in 3 countries.

Murat R GainullinCentral Research Laboratory, Nizhniy Novgorod State Medical Academy, Nizhniy Novgorod, Minin Sq. 10/1, 603005, Russia.
Ilya Yu ZhukovCentral Research Laboratory, Nizhniy Novgorod State Medical Academy, Nizhniy Novgorod, Minin Sq. 10/1, 603005, Russia.
Xiaoying ZhouMedical Research Center, Guangxi Medical University, Nanning, China.
Yingxi MoDepartment of Research, Affiliated Tumor Hospital of Guangxi Medical University, Nanning, China.
Lidiia AstakhovaDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Sweden.
Ingemar ErnbergDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Sweden.
Liudmila MatskovaDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Sweden. liudmila.matskova@ki.se.
Karolinska Institutet · SEGuangxi Medical University · CNN. I. Lobachevsky State University of Nizhny Novgorod · RUNizhny Novgorod State Pedagogical University · RUTumor Hospital of Guangxi Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Expression of cofilin is directly associated with metastatic activity in many tumors. Here, we studied the role of Latent Membrane Protein 2 A (LMP2A) of Epstein-Barr Virus (EBV) in the accumulation of cofilin observed in nasopharyngeal cancer (NPC) tumor cells. We used LMP2A transformed NPC cell lines to analyze cofilin expression. We used mutation analysis, ectopic expression and down-regulation of Cbl, AIP4 and Syk in these cell lines to determine the effect of the LMP2A viral protein on cofilin degradation and its role in the assembly of a cofilin degrading protein complex. The LMP2A of EBV was found to interfer with cofilin degradation in NPC cells by accelerating the proteasomal degradation of Cbl and Syk. In line with this, we found significantly higher cofilin expression in NPC tumor samples as compared to the surrounding epithelial tissues. Cofilin, as an actin severing protein, influences cellular plasticity, and facilitates cellular movement in response to oncogenic stimuli. Thus, under relaxed cellular control, cofilin facilitates tumor cell movement and dissemination. Interference with its degradation may enhance the metastatic potential of NPC cells.

Indexed as

Actin Depolymerizing FactorsCell Line, TumorHerpesvirus 4, HumanHost-Pathogen InteractionsHumansNasopharyngeal CarcinomaProteolysisProto-Oncogene Proteins c-cblRepressor ProteinsSyk KinaseUbiquitin-Protein LigasesViral Matrix ProteinsActin Depolymerizing FactorsCBL protein, humanEBV-associated membrane antigen, Epstein-Barr virusITCH protein, humanProto-Oncogene Proteins c-cblRepressor ProteinsSyk KinaseSYK protein, humanUbiquitin-Protein LigasesViral Matrix Proteins

Identifiers

PMID28827787
PMCPMC5567079
OpenAlexW2747074566

What OpenQuestion holds

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LicenceCC BY
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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.