Evidence map›Paper›PMID 29434030›Full record

ArticleThe Journal of cell biology2018

Src-mediated phosphorylation converts FHL1 from tumor suppressor to tumor promoter.

Xiang Wang, Xiaofan Wei, Yang Yuan, Qingrui Sun, Jun Zhan, Jing Zhang, Yan Tang, Feng Li, Lihua Ding, Qinong Ye and 1 more

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

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  12. Function of BCLAF1 in human disease.Oncology letters · 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

11 authors at 2 institutions in 1 country.

Xiang WangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Xiaofan WeiKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.ORCID 0000-0003-2151-9322
Yang YuanKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Qingrui SunKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Jun ZhanKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Jing ZhangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Yan TangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Feng LiKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China.
Lihua DingDepartment of Medical Molecular Biology, Beijing Institute of Biotechnology, Collaborative Innovation Center for Cancer Medicine, Beijing, China.
Qinong YeDepartment of Medical Molecular Biology, Beijing Institute of Biotechnology, Collaborative Innovation Center for Cancer Medicine, Beijing, China.
Hongquan ZhangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Human Anatomy, Histology and Embryology, and State Key Laboratory of Natural and Biomimetic Drugs, Peking University Health Science Center, Beijing, China Hongquan.Zhang@bjmu.edu.cn.ORCID 0000-0001-8193-0899
Ministry of Education of the People's Republic of China · CNPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FHL1 has been recognized for a long time as a tumor suppressor protein that associates with both the actin cytoskeleton and the transcriptional machinery. We present in this study a paradigm that phosphorylated FHL1 functions as an oncogenic protein by promoting tumor cell proliferation. The cytosolic tyrosine kinase Src interacts with and phosphorylates FHL1 at Y149 and Y272, which switches FHL1 from a tumor suppressor to a cell growth accelerator. Phosphorylated FHL1 translocates into the nucleus, where it binds to the transcription factor BCLAF1 and promotes tumor cell growth. Importantly, the phosphorylation of FHL1 is increased in tissues from lung adenocarcinoma patients despite the down-regulation of total FHL1 expression. Kindlin-2 was found to interact with FHL1 and recruit FHL1 to focal adhesions. Kindlin-2 competes with Src for binding to FHL1 and suppresses Src-mediated FHL1 phosphorylation. Collectively, we demonstrate that FHL1 can either suppress or promote tumor cell growth depending on the status of the sites for phosphorylation by Src.

Indexed as

Cell ProliferationActive Transport, Cell NucleusAdenocarcinoma of LungAnimalsBinding, CompetitiveCell MovementFemaleHeLa CellsHumansIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsLung NeoplasmsMembrane ProteinsMice, Inbred BALB CMice, NudeMuscle ProteinsBCLAF1 protein, humanFERMT3 protein, humanFHL1 protein, humanIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMembrane ProteinsMuscle ProteinsNeoplasm ProteinsRepressor Proteinssrc-Family KinasesTumor Suppressor Proteins

Identifiers

PMID29434030
PMCPMC5881501
OpenAlexW2786219994

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.