Evidence map›Paper›PMID 25378401›Full record

ArticleThe Journal of biological chemistry2014

NGX6a is degraded through a proteasome-dependent pathway without ubiquitination mediated by ezrin, a cytoskeleton-membrane linker.

Li Wang, Xiaoling Li, Bo Xiang, Ming Zhou, Xiayu Li, Wei Xiong, Man Niu, Pingpin Wei, Zeyou Wang, Heran Wang and 4 more

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

Article in The Journal of biological chemistry, 2014. 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
0.4field-weighted citation impact, top 35% 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, 4 citations in OpenAlex.

  1. Tumor suppressor NGX6 inhibits the growth and metastasis of multiple cancers.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    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

14 authors at 3 institutions in 1 country.

Li Wangthe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China, the Department of Cardio-Thoracic Surgery, Second Xiangya Hospital of Central South University, 139 Renmin Middle Road, Changsha, Hunan 410012, China, and.
Xiaoling Lithe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China, From the Hunan Provincial Tumor Hospital and the Affiliated Tumor Hospital of Xiangya School of Medicine, Central South University, 582 Xianjiahu Road, Changsha, Hunan 410013, China.
Bo Xiangthe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China, From the Hunan Provincial Tumor Hospital and the Affiliated Tumor Hospital of Xiangya School of Medicine, Central South University, 582 Xianjiahu Road, Changsha, Hunan 410013, China.
Ming Zhouthe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China, From the Hunan Provincial Tumor Hospital and the Affiliated Tumor Hospital of Xiangya School of Medicine, Central South University, 582 Xianjiahu Road, Changsha, Hunan 410013, China.
Xiayu Lithe Third Xiang-Ya Hospital, Central South University, Changsha, Hunan 410013, China.
Wei Xiongthe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China, From the Hunan Provincial Tumor Hospital and the Affiliated Tumor Hospital of Xiangya School of Medicine, Central South University, 582 Xianjiahu Road, Changsha, Hunan 410013, China.
Man Niuthe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China.
Pingpin Weithe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China.
Zeyou Wangthe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China.
Heran Wangthe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China.
Pan ChenFrom the Hunan Provincial Tumor Hospital and the Affiliated Tumor Hospital of Xiangya School of Medicine, Central South University, 582 Xianjiahu Road, Changsha, Hunan 410013, China.
Shourong Shenthe Third Xiang-Ya Hospital, Central South University, Changsha, Hunan 410013, China.
Shuping Pengthe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China, From the Hunan Provincial Tumor Hospital and the Affiliated Tumor Hospital of Xiangya School of Medicine, Central South University, 582 Xianjiahu Road, Changsha, Hunan 410013, China, shuping@csu.edu.cn.
Guiyuan Lithe Cancer Research Institute, Central South University, Changsha, Hunan 410078, China, From the Hunan Provincial Tumor Hospital and the Affiliated Tumor Hospital of Xiangya School of Medicine, Central South University, 582 Xianjiahu Road, Changsha, Hunan 410013, China, lgy@csu.edu.cn.
Central South University · CNHunan Cancer Hospital · CNSecond Xiangya Hospital of Central South University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Our previous study demonstrated that the NGX6b gene acts as a suppressor in the invasion and migration of nasopharyngeal carcinoma (NPC). Recently, we identified the novel isoform NGX6a, which is longer than NGX6b. In this study, we first found that NGX6a was degraded in NPC cells and that this degradation was mediated by ezrin, a linker between membrane proteins and the cytoskeleton. Specific siRNAs against ezrin increase the protein level of NGX6a in these cells. During degradation, NGX6a is not ubiquitinated but is degraded through a proteasome-dependent pathway. The distribution pattern of ezrin was negatively associated with NGX6a in an immunochemistry analysis of a nasopharyngeal carcinoma tissue microarray and fetus multiple organ tissues and Western blot analysis in nasopharyngeal and NPC cell lines, suggesting that ezrin and NGX6a are associated and are involved in the progression and invasion of NPC. By mapping the interacting binding sites, the seven-transmembrane domain of NGX6a was found to be the critical region for the degradation of NGX6a, and the amino terminus of ezrin is required for the induction of NGX6a degradation. The knockdown of ezrin or transfection of the NGX6a mutant CO, which has an EGF-like domain and a transmembrane 1 domain, resulted in no degradation, significantly reducing the ability of invasion and migration of NPC cells. This study provides a novel molecular mechanism for the low expression of NGX6a in NPC cells and an important molecular event in the process of invasion and metastasis of nasopharyngeal carcinoma cells.

Indexed as

CarcinomaCell Line, TumorCytoskeletal ProteinsCytoskeletonEzrinHumansMembrane ProteinsNasopharyngeal CarcinomaNasopharyngeal NeoplasmsProteasome Endopeptidase ComplexProtein Interaction Domains and MotifsProtein IsoformsProteolysisTumor Suppressor ProteinsUbiquitinationCytoskeletal ProteinsEzrinMembrane ProteinsProteasome Endopeptidase ComplexProtein IsoformsTMEM8B protein, humanTumor Suppressor ProteinsBiodegradationCancerDegradationEzrinMetastasisNasopharyngeal CarcinomaNGX6aUbiquitylation (Ubiquitination)

Identifiers

PMID25378401
PMCPMC4276843
OpenAlexW1971633700

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.