Evidence map›Paper›PMID 25245533›Full record

ArticleOncotarget2014

Interleukin-32α downregulates the activity of the B-cell CLL/lymphoma 6 protein by inhibiting protein kinase Cε-dependent SUMO-2 modification.

Yun Sun Park, Jeong-Woo Kang, Dong Hun Lee, Man Sub Kim, Yesol Bak, Young Yang, Hee Gu Lee, JinTae Hong, Do-Young Yoon

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Oncotarget, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

6 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

9 authors at 4 institutions in 1 country.

Yun Sun ParkDepartment of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, South Korea.
Jeong-Woo KangDepartment of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, South Korea.
Dong Hun LeeDepartment of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, South Korea.
Man Sub KimDepartment of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, South Korea.
Yesol BakDepartment of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, South Korea.
Young YangResearch Center for Women's Disease, Department of Life Systems, Sookmyung Women's University, Seoul, South Korea.
Hee Gu LeeMedical Genomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, South Korea.
JinTae HongCollege of Pharmacy and Medical Research Center, Chungbuk National University, Cheongju, South Korea.
Do-Young YoonDepartment of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, South Korea.
Konkuk University · KRChungbuk National University · KRKorea Research Institute of Bioscience and Biotechnology · KRSookmyung Women's University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A proinflammatory cytokine IL-32 acts as an intracellular mediator. IL-32α interacts with many intracellular molecules, but there are no reports of interaction with a transcriptional repressor BCL6. In this study, we showed that PMA induces an interaction between IL-32α, PKCε, and BCL6, forming a trimer. To identify the mechanism of the interaction, we treated cells with various inhibitors. In HEK293 and THP-1 cell lines, treatment with a pan-PKC inhibitor, PKCε inhibitor, and PKCδ inhibitor decreased BCL6 and IL-32α protein expression. MAPK inhibitors and classical PKC inhibitor did not decrease PMA-induced BCL6 and IL-32α protein expression. Further, the pan-PKC inhibitor and PKCε inhibitor disrupted PMA-induced interaction between IL-32α and BCL6. These data demonstrate that the intracellular interaction between IL-32α and BCL6 is induced by PMA-activated PKCε. PMA induces post-translational modification of BCL6 by conjugation to SUMO-2, while IL-32α inhibits. PKCε inhibition eliminated PMA-induced SUMOylation of BCL6. Inhibition of BCL6 SUMOylation by IL-32α affected the cellular function and activity of the transcriptional repressor BCL6 in THP-1 cells. Thus, we showed that IL-32α is a negative regulator of the transcriptional repressor BCL6. IL-32α inhibits BCL6 SUMOylation by activating PKCε, resulting in the modulation of BCL6 target genes and cellular functions of BCL6.

Indexed as

Cell Line, TumorDNA-Binding ProteinsDown-RegulationGene Expression Regulation, NeoplasticHEK293 CellsHumansInterleukinsLeukemiaProtein Kinase C-epsilonProtein Kinase InhibitorsProto-Oncogene Proteins c-bcl-6RNA InterferenceSignal TransductionSmall Ubiquitin-Related Modifier ProteinsSumoylationTetradecanoylphorbol AcetateBCL6 protein, humanDNA-Binding ProteinsIL32 protein, humanInterleukinsPRKCE protein, humanProtein Kinase C-epsilonProtein Kinase InhibitorsProto-Oncogene Proteins c-bcl-6Small Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanTetradecanoylphorbol Acetate

Identifiers

PMID25245533
PMCPMC4226720
OpenAlexW1589398617

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.