Evidence map›Paper›PMID 32576196›Full record

ArticleJournal of biomedical science2020

ZNF322A-mediated protein phosphorylation induces autophagosome formation through modulation of IRS1-AKT glucose uptake and HSP-elicited UPR in lung cancer.

Chantal Hoi Yin Cheung, Chia-Lang Hsu, Tsai-Yu Lin, Wei-Ting Chen, Yi-Ching Wang, Hsuan-Cheng Huang, Hsueh-Fen Juan

Open access · diamondAbstract read
In one paragraph

Article in Journal of biomedical science, 2020. 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
0.6field-weighted citation impact, top 35% 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, 10 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

7 authors at 3 institutions in 1 country.

Chantal Hoi Yin CheungDepartment of Life Science, National Taiwan University, Taipei, 10617, Taiwan.
Chia-Lang HsuDepartment of Life Science, National Taiwan University, Taipei, 10617, Taiwan.
Tsai-Yu LinDepartment of Life Science, National Taiwan University, Taipei, 10617, Taiwan.
Wei-Ting ChenDepartment of Life Science, National Taiwan University, Taipei, 10617, Taiwan.
Yi-Ching WangDepartment of Pharmacology, College of Medicine, National Cheng Kung University, Tainan, 70101, Taiwan.
Hsuan-Cheng HuangInstitute of Biomedical Informatics, National Yang-Ming University, No.155, Sec.2, Linong Street, Taipei, 11221, Taiwan. hsuancheng@ym.edu.tw.
Hsueh-Fen JuanDepartment of Life Science, National Taiwan University, Taipei, 10617, Taiwan. yukijuan@ntu.edu.tw.ORCID http://orcid.org/0000-0003-4876-3309
National Taiwan University · TWNational Cheng Kung University · TWNational Yang Ming Chiao Tung University · TW

Funding

Ministry of Science and Technology, Taiwan MOST 104-2627-B-002-001, MOST 106-2320-B-002-053-MY3Ministry of Science and Technology, Taiwan MOST107-2221-E-010-017-MY2Ministry of Science and Technology, Taiwan MOST 108-2321-B-006-002
6 · The paper itself

Abstract

backgroundZNF322A is an oncogenic transcription factor that belongs to the Cys2His2-type zinc-finger protein family. Accumulating evidence suggests that ZNF322A may contribute to the tumorigenesis of lung cancer, however, the ZNF322A-mediated downstream signaling pathways remain unknown.

methodsTo uncover ZNF322A-mediated functional network, we applied phosphopeptide enrichment and isobaric labeling strategies with mass spectrometry-based proteomics using A549 lung cancer cells, and analyzed the differentially expressed proteins of phosphoproteomic and proteomic profiles to determine ZNF322A-modulated pathways.

resultsZNF322A highlighted a previously unidentified insulin signaling, heat stress, and signal attenuation at the post-translational level. Consistently, protein-phosphoprotein-kinase interaction network analysis revealed phosphorylation of IRS1 and HSP27 were altered upon ZNF322A-silenced lung cancer cells. Thus, we further investigated the molecular regulation of ZNF322A, and found the inhibitory transcriptional regulation of ZNF322A on PIM3, which was able to phosphorylate IRS1 at serine

conclusionsThese findings not only give new information about the molecular regulation of the cellular proteins through ZNF322A at the post-translational level, but also provides a resource for the study of lung cancer therapy.

Indexed as

Unfolded Protein ResponseA549 CellsAutophagosomesHeat-Shock ProteinsHumansInsulin Receptor Substrate ProteinsLung NeoplasmsOncogene ProteinsPhosphorylationProto-Oncogene Proteins c-aktTranscription FactorsHeat-Shock ProteinsInsulin Receptor Substrate ProteinsIRS1 protein, humanOncogene ProteinsProto-Oncogene Proteins c-aktTranscription FactorsZNF322 protein, humanAutophagyGlucose starvationHeat stressLung cancerPhosphoproteomicsProteomicsZinc-finger protein

Identifiers

PMID32576196
PMCPMC7310457
OpenAlexW3036114744

What Socratic 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 Socratic graph.