Evidence map›Paper›PMID 25659434›Full record

ArticleThe Journal of biological chemistry2015

Phosphorylation of Krüppel-like factor 3 (KLF3/BKLF) and C-terminal binding protein 2 (CtBP2) by homeodomain-interacting protein kinase 2 (HIPK2) modulates KLF3 DNA binding and activity.

Vitri Dewi, Alister Kwok, Stella Lee, Ming Min Lee, Yee Mun Tan, Hannah R Nicholas, Kyo-ichi Isono, Beeke Wienert, Ka Sin Mak, Alexander J Knights and 5 more

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

Article in The Journal of biological chemistry, 2015. 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
1.1field-weighted citation impact, top 24% 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, 24 citations in OpenAlex.

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  6. Review
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  11. Krüppel-like factor 3 inhibition by mutated lncRNAThe Journal of experimental medicine · 2019
    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

15 authors at 3 institutions in 2 countries.

Vitri DewiFrom the School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia.
Alister Kwokthe School of Molecular Bioscience, University of Sydney, Sydney, New South Wales, 2006, Australia, and.
Stella Leethe School of Molecular Bioscience, University of Sydney, Sydney, New South Wales, 2006, Australia, and.
Ming Min Leethe School of Molecular Bioscience, University of Sydney, Sydney, New South Wales, 2006, Australia, and.
Yee Mun Tanthe School of Molecular Bioscience, University of Sydney, Sydney, New South Wales, 2006, Australia, and.
Hannah R Nicholasthe School of Molecular Bioscience, University of Sydney, Sydney, New South Wales, 2006, Australia, and.
Kyo-ichi Isonothe RIKEN Research Center for Allergy and Immunology, Tsurumi-ku, Yokohama City, Kanagawa 230-0045, Japan.
Beeke WienertFrom the School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia.
Ka Sin MakFrom the School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia.
Alexander J KnightsFrom the School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia.
Kate G R QuinlanFrom the School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia.
Stuart J Cordwellthe School of Molecular Bioscience, University of Sydney, Sydney, New South Wales, 2006, Australia, and.
Alister P W FunnellFrom the School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia.
Richard C M PearsonFrom the School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia.
Merlin CrossleyFrom the School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia, the School of Molecular Bioscience, University of Sydney, Sydney, New South Wales, 2006, Australia, and m.crossley@unsw.edu.au.
UNSW Sydney · AUUniversity of Sydney · AURIKEN Center for Integrative Medical Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Krüppel-like factor 3 (KLF3/BKLF), a member of the Krüppel-like factor (KLF) family of transcription factors, is a widely expressed transcriptional repressor with diverse biological roles. Although there is considerable understanding of the molecular mechanisms that allow KLF3 to silence the activity of its target genes, less is known about the signal transduction pathways and post-translational modifications that modulate KLF3 activity in response to physiological stimuli. We observed that KLF3 is modified in a range of different tissues and found that the serine/threonine kinase homeodomain-interacting protein kinase 2 (HIPK2) can both bind and phosphorylate KLF3. Mass spectrometry identified serine 249 as the primary phosphorylation site. Mutation of this site reduces the ability of KLF3 to bind DNA and repress transcription. Furthermore, we also determined that HIPK2 can phosphorylate the KLF3 co-repressor C-terminal binding protein 2 (CtBP2) at serine 428. Finally, we found that phosphorylation of KLF3 and CtBP2 by HIPK2 strengthens the interaction between these two factors and increases transcriptional repression by KLF3. Taken together, our results indicate that HIPK2 potentiates the activity of KLF3.

Indexed as

Alcohol OxidoreductasesAmino Acid SequenceAnimalsCarrier ProteinsChlorocebus aethiopsCo-Repressor ProteinsCOS CellsDNADNA-Binding ProteinsElectrophoretic Mobility Shift AssayKruppel-Like Transcription FactorsMiceMolecular Sequence DataNIH 3T3 CellsPhosphoproteinsPhosphorylationAlcohol OxidoreductasesCarrier ProteinsCo-Repressor ProteinsCtbp2 protein, mouseDNADNA-Binding ProteinsHipk2 protein, mouseKlf3 protein, mouseKruppel-Like Transcription FactorsPhosphoproteinsProtein Serine-Threonine KinasesC-terminal Binding Protein (CtBP2)Gene ExpressionHomeodomain-interacting Protein Kinase 2 (HIPK2)Kruppel-like Factor 3 (KLF3/BKLF)Kruppel-like Factor (KLF)Post-translational Modification (PTM)Protein PhosphorylationTranscription Regulation

Identifiers

PMID25659434
PMCPMC4375508
OpenAlexW2011288527

What OpenQuestion holds

Textmetadata
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.