Evidence map›Paper›PMID 27212225›Full record

ArticleScientific reports2016

Suppression of 14-3-3γ-mediated surface expression of ANO1 inhibits cancer progression of glioblastoma cells.

Young-Sun Lee, Jae Kwang Lee, Yeonju Bae, Bok-Soon Lee, Eunju Kim, Chang-Hoon Cho, Kanghyun Ryoo, Jiyun Yoo, Chul-Ho Kim, Gwan-Su Yi and 5 more

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

35 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  5. Review
  6. TMEM16 proteins: CaInternational journal of molecular medicine · 2024
    Review
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  12. Role of ANO1 in tumors and tumor immunity.Journal of cancer research and clinical oncology · 2022
    Review
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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

15 authors.

Young-Sun LeeSchool of Biosystem and Biomedical Science, College of Health Science, Korea University, Seoul 02841, Republic of Korea.
Jae Kwang LeeNeuroscience Program, University of Science and Technology (UST), Daejeon 34113, Republic of Korea.
Yeonju BaeSchool of Biosystem and Biomedical Science, College of Health Science, Korea University, Seoul 02841, Republic of Korea.
Bok-Soon LeeDepartment of Otolaryngology, Ajou University School of Medicine, Suwon 16499, Republic of Korea.
Eunju KimSchool of Biosystem and Biomedical Science, College of Health Science, Korea University, Seoul 02841, Republic of Korea.
Chang-Hoon ChoSchool of Biosystem and Biomedical Science, College of Health Science, Korea University, Seoul 02841, Republic of Korea.
Kanghyun RyooSchool of Biosystem and Biomedical Science, College of Health Science, Korea University, Seoul 02841, Republic of Korea.
Jiyun YooDivision of Applied Life Science (BK21 plus), Research Institute of Life Sciences, Gyeongsang National University, Jinju 52828, Korea.
Chul-Ho KimDepartment of Otolaryngology, Ajou University School of Medicine, Suwon 16499, Republic of Korea.
Gwan-Su YiDepartment of Bio and Brain Engineering, KAIST, Daejeon 34141, Republic of Korea.
Seok-Geun LeeDepartment of Science in Korean Medicine, College of Korean Medicine, KHU-KIST department of Convergging Science and Technology, Kyung Hee University, Seoul 02447, Republic of Korea.
C Justin LeeCenter for Functional Connectomics, Korea Institute of Science and Technology (KIST), Seoul 02792, Republic of Korea.
Sang Soo KangDepartment of Anatomy and Convergence Medical Science, Institute of Health Sciences, School of Medicine, Gyeongsang National University, Jinju 52727, Republic of Korea.
Eun Mi HwangCenter for Functional Connectomics, Korea Institute of Science and Technology (KIST), Seoul 02792, Republic of Korea.
Jae-Yong ParkSchool of Biosystem and Biomedical Science, College of Health Science, Korea University, Seoul 02841, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anoctamin-1 (ANO1) acts as a Ca(2+)-activated Cl(-) channel in various normal tissues, and its expression is increased in several different types of cancer. Therefore, understanding the regulation of ANO1 surface expression is important for determining its physiological and pathophysiological functions. However, the trafficking mechanism of ANO1 remains elusive. Here, we report that segment a (N-terminal 116 amino acids) of ANO1 is crucial for its surface expression, and we identified 14-3-3γ as a binding partner for anterograde trafficking using yeast two-hybrid screening. The surface expression of ANO1 was enhanced by 14-3-3γ, and the Thr9 residue of ANO1 was critical for its interaction with 14-3-3γ. Gene silencing of 14-3-3γ and/or ANO1 demonstrated that suppression of ANO1 surface expression inhibited migration and invasion of glioblastoma cells. These findings provide novel therapeutic implications for glioblastomas, which are associated with poor prognosis.

Indexed as

14-3-3 ProteinsAnoctamin-1Binding SitesBrain NeoplasmsCell Line, TumorCell MembraneCell MovementDisease ProgressionGene Expression Regulation, NeoplasticGlioblastomaHEK293 CellsHumansNeoplasm InvasivenessNeoplasm ProteinsProtein BindingTwo-Hybrid System Techniques14-3-3 ProteinsANO1 protein, humanAnoctamin-1Neoplasm ProteinsYWHAG protein, human

Identifiers

PMID27212225
PMCPMC4876403

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Registered trials

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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.