Evidence map›Paper›PMID 20100835›Full record

ArticleThe Journal of biological chemistry2010

Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm.

Yun-Mi Goh, Senthilkumar Cinghu, Eileen Tan Hwee Hong, You-Soub Lee, Jang-Hyun Kim, Ju-Won Jang, Ying-Hui Li, Xin-Zi Chi, Kyeong-Sook Lee, Heejun Wee and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

30 citing papers in PubMed, 54 citations in OpenAlex.

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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

13 authors at 3 institutions in 3 countries.

Yun-Mi GohDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Senthilkumar CinghuDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Eileen Tan Hwee HongCancer Science Institute Singapore, National University of Singapore and Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore.
You-Soub LeeDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Jang-Hyun KimDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Ju-Won JangDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Ying-Hui LiDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Xin-Zi ChiDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Kyeong-Sook LeeDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Heejun WeeDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea.
Yoshiaki ItoCancer Science Institute Singapore, National University of Singapore and Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore.
Byung-Chul OhLee Gil Ya Cancer and Diabetes Institute, Gachon University of Medicine and Science, 7-45 Songdo-dong, Yeonsu-ku, Inchon 406-840, South Korea. Electronic address: bcoh@gachon.ac.kr.
Suk-Chul BaeDepartment of Biochemistry, School of Medicine, Institute for Tumor Research, Chungbuk National University, Cheongju 361-763, South Korea. Electronic address: scbae@chungbuk.ac.kr.
Chungbuk National University · KRNational University of Singapore · SGCharles R. Drew University of Medicine and Science · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RUNX3 is a transcription factor that functions as a tumor suppressor. In some cancers, RUNX3 expression is down-regulated, usually due to promoter hypermethylation. Recently, it was found that RUNX3 can also be inactivated by the mislocalization of the protein in the cytoplasm. The molecular mechanisms controlling this mislocalization are poorly understood. In this study, we found that the overexpression of Src results in the tyrosine phosphorylation and cytoplasmic localization of RUNX3. We also found that the tyrosine residues of endogenous RUNX3 are phosphorylated and that the protein is localized in the cytoplasm in Src-activated cancer cell lines. We further showed that the knockdown of Src by small interfering RNA, or the inhibition of Src kinase activity by a chemical inhibitor, causes the re-localization of RUNX3 to the nucleus. Collectively, our results demonstrate that the tyrosine phosphorylation of RUNX3 by activated Src is associated with the cytoplasmic localization of RUNX3 in gastric and breast cancers.

Indexed as

Gene Expression Regulation, NeoplasticBreast NeoplasmsCell Line, TumorCell NucleusCore Binding Factor Alpha 3 SubunitCytoplasmHeLa CellsHumansPhosphorylationProtein TransportRNA, Small Interferingsrc-Family KinasesStomach NeoplasmsTyrosineCore Binding Factor Alpha 3 SubunitRNA, Small InterferingRunx3 protein, humansrc-Family KinasesTyrosine

Identifiers

PMID20100835
PMCPMC2843174
OpenAlexW2090447171

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.