Evidence map›Paper›PMID 34675258›Full record

ArticleScientific reports2021

TCTP protein degradation by targeting mTORC1 and signaling through S6K, Akt, and Plk1 sensitizes lung cancer cells to DNA-damaging drugs.

Mini Jeong, Mi Hyeon Jeong, Jung Eun Kim, Serin Cho, Kyoung Jin Lee, Serkin Park, Jeongwon Sohn, Yun Gyu Park

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

8 citing papers in PubMed, 9 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

8 authors at 1 institution in 1 country.

Mini Jeong *Department of Biochemistry and Molecular Biology, Korea University College of Medicine, 73 Koryodae-ro, Sungbuk-gu, Seoul, 02841, Republic of Korea.
Mi Hyeon Jeong *Department of Biochemistry and Molecular Biology, Korea University College of Medicine, 73 Koryodae-ro, Sungbuk-gu, Seoul, 02841, Republic of Korea.
Jung Eun KimDepartment of Biochemistry and Molecular Biology, Korea University College of Medicine, 73 Koryodae-ro, Sungbuk-gu, Seoul, 02841, Republic of Korea.
Serin ChoDepartment of Biochemistry and Molecular Biology, Korea University College of Medicine, 73 Koryodae-ro, Sungbuk-gu, Seoul, 02841, Republic of Korea.
Kyoung Jin LeeDepartment of Biochemistry and Molecular Biology, Korea University College of Medicine, 73 Koryodae-ro, Sungbuk-gu, Seoul, 02841, Republic of Korea.
Serkin ParkDepartment of Biochemistry and Molecular Biology, Korea University College of Medicine, 73 Koryodae-ro, Sungbuk-gu, Seoul, 02841, Republic of Korea.
Jeongwon SohnDepartment of Biochemistry and Molecular Biology, Korea University College of Medicine, 73 Koryodae-ro, Sungbuk-gu, Seoul, 02841, Republic of Korea.
Yun Gyu ParkDepartment of Biochemistry and Molecular Biology, Korea University College of Medicine, 73 Koryodae-ro, Sungbuk-gu, Seoul, 02841, Republic of Korea. parkyg@korea.ac.kr.
Korea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translationally controlled tumor protein (TCTP) is expressed in many tissues, particularly in human tumors. It plays a role in malignant transformation, apoptosis prevention, and DNA damage repair. The signaling mechanisms underlying TCTP regulation in cancer are only partially understood. Here, we investigated the role of mTORC1 in regulating TCTP protein levels, thereby modulating chemosensitivity, in human lung cancer cells and an A549 lung cancer xenograft model. The inhibition of mTORC1, but not mTORC2, induced ubiquitin/proteasome-dependent TCTP degradation without a decrease in the mRNA level. PLK1 activity was required for TCTP ubiquitination and degradation and for its phosphorylation at Ser

Indexed as

A549 CellsAnimalsAntineoplastic AgentsCell Cycle ProteinsDNA DamageHumansLung NeoplasmsMaleMechanistic Target of Rapamycin Complex 1MiceMice, Inbred BALB CMice, NudePolo-Like Kinase 1Protein Serine-Threonine KinasesProteolysisProto-Oncogene ProteinsAntineoplastic AgentsCell Cycle ProteinsMechanistic Target of Rapamycin Complex 1Polo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRibosomal Protein S6 KinasesTPT1 protein, humanTumor Protein, Translationally-Controlled 1

Identifiers

PMID34675258
PMCPMC8531033
OpenAlexW3205067550

What OpenQuestion holds

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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.