Evidence map›Paper›PMID 29570932›Full record

ArticleMolecular oncology2018

PIM2 interacts with tristetraprolin and promotes breast cancer tumorigenesis.

Chune Ren, Tingting Yang, Pengyun Qiao, Li Wang, Xue Han, Shijun Lv, Yonghong Sun, Zhijun Liu, Yu Du, Zhenhai Yu

Open access · goldAbstract read
In one paragraph

Article in Molecular oncology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

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  9. Synthesis of 2-Oxoquinoline Derivatives as Dual Pim and mTORC Protein Kinase Inhibitors.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2022
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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

10 authors at 1 institution in 1 country.

Chune RenDepartment of Reproductive Medicine, Affiliated Hospital of Weifang Medical University, Shandong, China.
Tingting YangDepartment of Reproductive Medicine, Affiliated Hospital of Weifang Medical University, Shandong, China.
Pengyun QiaoDepartment of Reproductive Medicine, Affiliated Hospital of Weifang Medical University, Shandong, China.
Li WangDepartment of Reproductive Medicine, Affiliated Hospital of Weifang Medical University, Shandong, China.
Xue HanDepartment of Reproductive Medicine, Affiliated Hospital of Weifang Medical University, Shandong, China.
Shijun LvDepartment of Pathology, Affiliated Hospital of Weifang Medical University, Shandong, China.
Yonghong SunDepartment of Pathology, Affiliated Hospital of Weifang Medical University, Shandong, China.
Zhijun LiuDepartment of Medical Biology, Weifang Medical University, Shandong, China.
Yu DuDepartment of Medical Biology, Weifang Medical University, Shandong, China.
Zhenhai YuDepartment of Reproductive Medicine, Affiliated Hospital of Weifang Medical University, Shandong, China.
Weifang Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tristetraprolin (TTP) is an AU-rich element-binding protein that regulates mRNA stability and plays important roles in cancer. The mechanisms by which TTP is regulated in breast cancer are poorly understood. Using multiple biochemical approaches, we found that proviral insertion in murine lymphomas 2 (PIM2) is a novel binding partner of TTP. Interestingly, PIM2 decreased TTP protein levels independent of its kinase activity. PIM2 instead targeted TTP protein for degradation via the ubiquitin-proteasome pathway. Furthermore, immunohistochemical staining showed that PIM2 and TTP protein levels were negatively correlated in human breast cancer samples. Indeed, PIM2 overexpression de-repressed TTP-mediated inhibition of breast cancer cell proliferation and migration in vitro and promoted breast tumor xenograft growth in vivo. These findings demonstrate an important role for the PIM2-TTP complex in breast cancer tumorigenesis, suggesting that PIM2 may represent a potential therapeutic target for breast cancer treatment.

Indexed as

AdultAnimalsBreast NeoplasmsCarcinogenesisCell LineCell MovementCell ProliferationFemaleGene Expression Regulation, NeoplasticHumansMice, NudeMiddle AgedProteasome Endopeptidase ComplexProtein BindingProtein DomainsProtein Serine-Threonine KinasesPIM2 protein, humanProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesProto-Oncogene ProteinsRNA, MessengerTristetraprolinUbiquitincancercell proliferationdegradationproviral insertion in murine lymphomas 2tristetraprolin

Identifiers

PMID29570932
PMCPMC5928357
OpenAlexW2791408484

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.