Evidence map›Paper›PMID 31446747›Full record

ArticleMolecules and cells2019

Phosphoserine Phosphatase Promotes Lung Cancer Progression through the Dephosphorylation of IRS-1 and a Noncanonical L-Serine-Independent Pathway.

Seong-Min Park, Eun-Hye Seo, Dong-Hyuck Bae, Sung Soo Kim, Jina Kim, Weiwei Lin, Kyung-Hee Kim, Jong Bae Park, Yong Sung Kim, Jinlong Yin and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecules and cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.7field-weighted citation impact, top 36% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  8. TiInternational journal of nanomedicine · 2025
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  13. ABRO1 arrests cardiomyocyte proliferation and myocardial repair by suppressing PSPH.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
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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 4 institutions in 2 countries.

Seong-Min ParkPersonalized Genomic Medicine Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 34141, Korea.
Eun-Hye SeoGenome Editing Research Center, KRIBB, Daejeon 34141, Korea.
Dong-Hyuck BaeGenome Editing Research Center, KRIBB, Daejeon 34141, Korea.
Sung Soo KimDepartment of Cancer Biomedical Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang 10408, Korea.
Jina KimPersonalized Genomic Medicine Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 34141, Korea.
Weiwei LinDepartment of Cancer Biomedical Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang 10408, Korea.
Kyung-Hee KimDepartment of Cancer Biomedical Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang 10408, Korea.
Jong Bae ParkDepartment of Cancer Biomedical Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang 10408, Korea.
Yong Sung KimGenome Editing Research Center, KRIBB, Daejeon 34141, Korea.
Jinlong YinHenan and Macquarie University Joint Centre for Biomedical Innovation, School of Life Sciences, Henan University, Kaifeng 475004, China.
Seon-Young KimPersonalized Genomic Medicine Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB), Daejeon 34141, Korea.
National Cancer Center · KRKorea Research Institute of Bioscience and Biotechnology · KRKorea University of Science and Technology · KRHenan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoserine phosphatase (PSPH) is one of the key enzymes of the L-serine synthesis pathway. PSPH is reported to affect the progression and survival of several cancers in an L-serine synthesis-independent manner, but the mechanism remains elusive. We demonstrate that PSPH promotes lung cancer progression through a noncanonical L-serine-independent pathway. PSPH was significantly associated with the prognosis of lung cancer patients and regulated the invasion and colony formation of lung cancer cells. Interestingly, L-serine had no effect on the altered invasion and colony formation by PSPH. Upon measuring the phosphatase activity of PSPH on a serine-phosphorylated peptide, we found that PSPH dephosphorylated phospho-serine in peptide sequences. To identify the target proteins of PSPH, we analyzed the protein phosphorylation profile and the PSPH-interacting protein profile using proteomic analyses and found one putative target protein, IRS-1. Immunoprecipitation and immunoblot assays validated a specific interaction between PSPH and IRS1 and the dephosphorylation of phospho-IRS-1 by PSPH in lung cancer cells. We suggest that the specific interaction and dephosphorylation activity of PSPH have novel therapeutic potential for lung cancer treatment, while the metabolic activity of PSPH, as a therapeutic target, is controversial.

Indexed as

Disease ProgressionA549 CellsAnimalsHumansInsulin Receptor Substrate ProteinsLung NeoplasmsMiceNeoplasm InvasivenessPhosphoric Monoester HydrolasesPhosphorylationSerineSignal TransductionSurvival AnalysisTumor Stem Cell AssayInsulin Receptor Substrate ProteinsPhosphoric Monoester Hydrolasesphosphoserine phosphataseSerineIRS-1L-serine independent pathwaylung cancerphosphoserine phosphatase

Identifiers

PMID31446747
PMCPMC6715339
OpenAlexW2981206437

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.