Evidence map›Paper›PMID 26183061›Full record

ArticleNature communications2015

PI3K/AKT activation induces PTEN ubiquitination and destabilization accelerating tumourigenesis.

Min-Sik Lee, Man-Hyung Jeong, Hyun-Woo Lee, Hyun-Ji Han, Aram Ko, Stephen M Hewitt, Jae-Hoon Kim, Kyung-Hee Chun, Joon-Yong Chung, Cheolju Lee and 2 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

117 citing papers in PubMed, 170 citations in OpenAlex.

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57 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 2 countries.

Min-Sik LeeDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
Man-Hyung JeongDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
Hyun-Woo LeeDepartment of Biochemistry and Molecular Biology, Yonsei University College of Medicine, Seoul 120-752, Republic of Korea.
Hyun-Ji HanDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
Aram KoDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
Stephen M HewittExperimental Pathology Laboratory, Center for Cancer Research, National Cancer Institute, NIH MSC 1500, Bethesda, Maryland 20892, USA.
Jae-Hoon Kim1] Department of Obstetrics and Gynecology, Gangnam Severance Hospital, Yonsei University College of Medicine, Seoul 135-720, Republic of Korea [2] Institute of Women's Life Medical Science, Yonsei University College of Medicine, Seoul 120-752, Republic of Korea.
Kyung-Hee ChunDepartment of Biochemistry and Molecular Biology, Yonsei University College of Medicine, Seoul 120-752, Republic of Korea.
Joon-Yong ChungExperimental Pathology Laboratory, Center for Cancer Research, National Cancer Institute, NIH MSC 1500, Bethesda, Maryland 20892, USA.
Cheolju LeeBRI, Korea Institute of Science and Technology, Seoul 136-791, Korea.
Hanbyoul Cho1] Department of Obstetrics and Gynecology, Gangnam Severance Hospital, Yonsei University College of Medicine, Seoul 135-720, Republic of Korea [2] Institute of Women's Life Medical Science, Yonsei University College of Medicine, Seoul 120-752, Republic of Korea.
Jaewhan SongDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
Yonsei University · KRNational Cancer Institute · USGangnam Severance Hospital · KRKorea Institute of Science & Technology Information · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activity of the phosphatase and tensin homologue (PTEN) is known to be suppressed via post-translational modification. However, the mechanism and physiological significance by which post-translational modifications lead to PTEN suppression remain unclear. Here we demonstrate that PTEN destabilization is induced by EGFR- or oncogenic PI3K mutation-mediated AKT activation in cervical cancer. EGFR/PI3K/AKT-mediated ubiquitination and degradation of PTEN are dependent on the MKRN1 E3 ligase. These processes require the stabilization of MKRN1 via AKT-mediated phosphorylation. In cervical cancer patients with high levels of pAKT and MKRN1 expression, PTEN protein levels are low and correlate with a low 5-year survival rate. Taken together, our results demonstrate that PI3K/AKT signals enforce positive-feedback regulation by suppressing PTEN function.

Indexed as

Gene Expression Regulation, NeoplasticAdenocarcinomaCarcinogenesisCarcinomaCarcinoma, Squamous CellCell Line, TumorCell MovementErbB ReceptorsFeedback, PhysiologicalFemaleHeLa CellsHumansImmunohistochemistryIn Vitro TechniquesMutationNerve Tissue ProteinsEGFR protein, humanErbB ReceptorsMakorin ring finger protein 1MTOR protein, humanNerve Tissue ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePTEN protein, humanRibonucleoproteinsTOR Serine-Threonine Kinases

Identifiers

PMID26183061
PMCPMC4518267
OpenAlexW2267081439

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.