Evidence map›Paper›PMID 28717195›Full record

ArticleScientific reports2017

Stability of the PHF10 subunit of PBAF signature module is regulated by phosphorylation: role of β-TrCP.

Victor V Tatarskiy, Yuriy P Simonov, Dmitrii S Shcherbinin, Alexander V Brechalov, Sofia G Georgieva, Nataliya V Soshnikova

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
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  4. The role of the polybromo-associated BAF complex in development.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2025
    Review
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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

6 authors at 4 institutions in 1 country.

Victor V TatarskiyLaboratory of Tumor Cell Death, N.N. Blokhin Russian Cancer Research Center, Kashirskoye Shosse 24, Moscow, 115478, Russia.ORCID 0000-0002-9080-5683
Yuriy P SimonovDepartment of Transcription Factors, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Str. 32, Moscow, 119991, Russia.
Dmitrii S ShcherbininLaboratory of Structure Bioinformatics, Institute of Biomedical Chemistry (IBMC), Pogodinskaya street 10 building 8, Moscow, 119121, Russia.
Alexander V BrechalovDepartment of Transcription Factors, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Str. 32, Moscow, 119991, Russia.
Sofia G GeorgievaDepartment of Eukariotic Transcription Factors, Institute of Gene Biology, Russian Academy of Sciences, Vavilov Str. 34/5, Moscow, 119991, Russia. sonjag@molbiol.edu.ru.
Nataliya V SoshnikovaDepartment of Eukariotic Transcription Factors, Institute of Gene Biology, Russian Academy of Sciences, Vavilov Str. 34/5, Moscow, 119991, Russia. so2615nat@gmail.com.
Engelhardt Institute of Molecular Biology · RUBioinformatics Institute · RUInstitute of Gene Biology · RURussian Cancer Research Center NN Blokhin · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PBAF chromatin-remodeling complexes are multi-protein machines, regulating expression of genes involved in proliferation and differentiation. PHF10 is a subunit of the PBAF essential for its association with chromatin. Mammalian PHF10 is expressed as four ubiquitous isoforms, which are alternatively incorporated in the complex and differ by their influence on transcription of target genes. PHF10 have different domain structure and two of them (PHF10-S isoforms) lack C-terminal PHD domains, which enables their phosphorylation by CK-1. Here we have found that PBAF subunits have low turnover rate, except for PHF10 which has much lower half-life, and is degraded by β-TrCP. The β-TrCP knockdown stabilizes PBAF core subunits - BRG1 and BAF155 and specific subunits - PHF10, BAF200, BAF180 and BRD7. PHF10 isoforms contain two non-canonical β-TrCP degrons and are degraded by β-TrCP in a phospho-dependent manner. But phosphorylation of PHF10-S degrons by CK-1, contrary to previously described degrons, prevents their degradation. Targeted molecular docking demonstrated that phosphorylated forms of PHF10 bind to β-TrCP with much lower affinity than non-phosphorylated ones, contrary to previously described degrons. This unorthodox mechanism proposes that phosphorylation of β-TrCP degrons by CK-1 could not only degrade a set of proteins, but also stabilize a different set of targets.

Indexed as

beta-Transducin Repeat-Containing ProteinsChromosomal Proteins, Non-HistoneGene Expression RegulationGene Knockdown TechniquesHalf-LifeHEK293 CellsHomeodomain ProteinsHumansModels, MolecularMolecular Docking SimulationNeoplasm ProteinsPhosphorylationProtein ConformationProtein DomainsProtein IsoformsProtein Stabilitybeta-Transducin Repeat-Containing ProteinsChromosomal Proteins, Non-HistoneHomeodomain ProteinsNeoplasm ProteinsPHF10 protein, humanProtein IsoformsSWI-SNF-B chromatin-remodeling complexTranscription Factors

Identifiers

PMID28717195
PMCPMC5514133
OpenAlexW2734809393

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Registered trials

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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.