Evidence map›Paper›PMID 29072687›Full record

ArticleCell death & disease2017

Guanylate-binding protein 2 regulates Drp1-mediated mitochondrial fission to suppress breast cancer cell invasion.

Juan Zhang, Yu Zhang, Wenshuang Wu, Fang Wang, Xinyu Liu, Guanghou Shui, Chunlai Nie

Erratum issuedAbstract read
In one paragraph

Article in Cell death & disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

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

  1. Pooled it
  2. Review
  3. Enhanced antitumor efficacy of combined targeting of adenosine ACancer immunology, immunotherapy : CII · 2026
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  5. Review
  6. Multifaceted Roles of Guanylate-Binding Proteins in Cancer.International journal of molecular sciences · 2025
    Review
  7. Cell-Autonomous Immunity: From Cytosolic Sensing to Self-Defense.International journal of molecular sciences · 2025
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Juan ZhangCenter for Core Facility and Advanced Technologies, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
Yu ZhangDepartment of Oncology, Guizhou People's Hospital, Guizhou 550002, China.
Wenshuang WuState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University and Collaborative Innovation Center for Biotherapy, Chengdu 610041, China.
Fang WangState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University and Collaborative Innovation Center for Biotherapy, Chengdu 610041, China.
Xinyu LiuState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University and Collaborative Innovation Center for Biotherapy, Chengdu 610041, China.
Guanghou ShuiState Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
Chunlai NieCenter for Core Facility and Advanced Technologies, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Guanylate-binding protein 2 (GBP2) is a member of the large GTPase superfamily that is strongly induced by interferon-γ (IFN-γ). Although the biochemical characteristics of GBP2 have been reported in detail, its biological function has not been thoroughly elucidated to date. To the best of our knowledge, this study presents the first demonstration that GBP2 inhibits mitochondrial fission and cell metastasis in breast cancer cells both in vitro and in vivo. Our previous work demonstrated that dynamin-related protein 1 (Drp1)-dependent mitochondrial fission has a key role in breast cancer cell invasion. In this study, we demonstrate that GBP2 binds directly to Drp1. Elimination of Drp1 by shRNA or Mdivi-1 (a Drp1-specific inhibitor) suppressed GBP2's regulatory function. Furthermore, GBP2 blocks Drp1 translocation from the cytosol to mitochondria, thereby attenuating Drp1-dependent mitochondrial fission and breast cancer cell invasion. In summary, our data provide new insights into the function and molecular mechanisms underlying GBP2's regulation of breast cancer cell invasion.

Indexed as

AnimalsBreast NeoplasmsCell Line, TumorDynaminsFemaleGTP-Binding ProteinsGTP PhosphohydrolasesHumansMiceMice, Inbred BALB CMice, NudeMicrotubule-Associated ProteinsMitochondriaMitochondrial ProteinsNeoplasm InvasivenessNIH 3T3 CellsDNM1L protein, humanDynaminsGBP2 protein, humanGTP-Binding ProteinsGTP PhosphohydrolasesMicrotubule-Associated ProteinsMitochondrial Proteins

Identifiers

PMID29072687
PMCPMC5680924

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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.