Evidence map›Paper›PMID 32789168›Full record

ArticleScience advances2020

BNIP-2 retards breast cancer cell migration by coupling microtubule-mediated GEF-H1 and RhoA activation.

Meng Pan, Ti Weng Chew, Darren Chen Pei Wong, Jingwei Xiao, Hui Ting Ong, Jasmine Fei Li Chin, Boon Chuan Low

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  4. Up-regulation of NGEF via the BRAFBiochemistry and biophysics reports · 2025
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  19. Structural basis for p50RhoGAP BCH domain-mediated regulation of Rho inactivation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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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

7 authors at 1 institution in 1 country.

Meng PanMechanobiology Institute, 5A Engineering Drive 1, National University of Singapore, Singapore 117411, Singapore.ORCID 0000-0002-8723-4824
Ti Weng ChewMechanobiology Institute, 5A Engineering Drive 1, National University of Singapore, Singapore 117411, Singapore.ORCID 0000-0002-5898-4722
Darren Chen Pei WongMechanobiology Institute, 5A Engineering Drive 1, National University of Singapore, Singapore 117411, Singapore.ORCID 0000-0002-1627-5792
Jingwei XiaoMechanobiology Institute, 5A Engineering Drive 1, National University of Singapore, Singapore 117411, Singapore.ORCID 0000-0003-1504-018X
Hui Ting OngMechanobiology Institute, 5A Engineering Drive 1, National University of Singapore, Singapore 117411, Singapore.
Jasmine Fei Li ChinMechanobiology Institute, 5A Engineering Drive 1, National University of Singapore, Singapore 117411, Singapore.
Boon Chuan LowMechanobiology Institute, 5A Engineering Drive 1, National University of Singapore, Singapore 117411, Singapore.ORCID 0000-0003-0756-096X
National University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules display dynamic turnover during cell migration, leading to cell contractility and focal adhesion maturation regulated by Rho guanosine triphosphatase activity. This interplay between microtubules and actomyosin is mediated by guanine nucleotide exchange factor (GEF)-H1 released after microtubule depolymerization or microtubule disconnection from focal adhesions. However, how GEF-H1 activates Rho upon microtubule disassembly remains elusive. Here, we found that BNIP-2, a BCH domain-containing protein that binds both RhoA and GEF-H1 and traffics with kinesin-1 on microtubules, is important for GEF-H1-driven RhoA activation upon microtubule disassembly. Depletion of BNIP-2 in MDA-MB-231 breast cancer cells decreases RhoA activity and promotes cell migration. Upon nocodazole-induced microtubule disassembly, the interaction between BNIP-2 and GEF-H1 increases, while knockdown of BNIP-2 reduces RhoA activation and cell rounding via uncoupling RhoA-GEF-H1 interaction. Together, these findings revealed that BNIP-2 couples microtubules and focal adhesions via scaffolding GEF-H1 and RhoA, fine-tuning RhoA activity and cell migration.

Indexed as

Breast NeoplasmsCarrier ProteinsCell MovementFemaleHumansMicrotubulesNocodazolerhoA GTP-Binding ProteinRho Guanine Nucleotide Exchange FactorsBNIP2 protein, humanCarrier ProteinsNocodazolerhoA GTP-Binding ProteinRHOA protein, humanRho Guanine Nucleotide Exchange Factors

Identifiers

PMID32789168
PMCPMC7399486
OpenAlexW3046895479

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.