Evidence map›Paper›PMID 21338522›Full record

ArticleMolecular cancer2011

PIAS1 interacts with FLASH and enhances its co-activation of c-Myb.

Anne Hege Alm-Kristiansen, Petra I Lorenzo, Ann-Kristin Molværsmyr, Vilborg Matre, Marit Ledsaak, Thomas Sæther, Odd S Gabrielsen

Open access · goldAbstract read
In one paragraph

Article in Molecular cancer, 2011. 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
1.7field-weighted citation impact, top 16% 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, 28 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 1 institution in 1 country.

Anne Hege Alm-KristiansenDepartment of Molecular Biosciences, University of Oslo, N-0316 Oslo, Norway.
Petra I Lorenzo
Ann-Kristin Molværsmyr
Vilborg Matre
Marit Ledsaak
Thomas Sæther
Odd S Gabrielsen
University of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFLASH is a huge nuclear protein involved in various cellular functions such as apoptosis signalling, NF-κB activation, S-phase regulation, processing of histone pre-mRNAs, and co-regulation of transcription. Recently, we identified FLASH as a co-activator of the transcription factor c-Myb and found FLASH to be tightly associated with active transcription foci. As a huge multifunctional protein, FLASH is expected to have many interaction partners, some which may shed light on its function as a transcriptional regulator.

resultsTo find additional FLASH-associated proteins, we performed a yeast two-hybrid (Y2H) screening with FLASH as bait and identified the SUMO E3 ligase PIAS1 as an interaction partner. The association appears to involve two distinct interaction surfaces in FLASH. We verified the interaction by Y2H-mating, GST pulldowns, co-IP and ChIP. FLASH and PIAS1 were found to co-localize in nuclear speckles. Functional assays revealed that PIAS1 enhances the intrinsic transcriptional activity of FLASH in a RING finger-dependent manner. Furthermore, PIAS1 also augments the specific activity of c-Myb, and cooperates with FLASH to further co-activate c-Myb. The three proteins, FLASH, PIAS1, and c-Myb, are all co-localized with active RNA polymerase II foci, resembling transcription factories.

conclusionsWe conclude that PIAS1 is a common partner for two cancer-related nuclear factors, c-Myb and FLASH. Our results point to a functional cooperation between FLASH and PIAS1 in the enhancement of c-Myb activity in active nuclear foci.

Indexed as

AnimalsApoptosis Regulatory ProteinsCalcium-Binding ProteinsCell NucleusChlorocebus aethiopsChromatinCOS CellsGene Expression RegulationHumansProtein BindingProtein Inhibitors of Activated STATProtein TransportProto-Oncogene Proteins c-mybRNA Polymerase IISmall Ubiquitin-Related Modifier ProteinsApoptosis Regulatory ProteinsCalcium-Binding ProteinsCASP8AP2 protein, humanChromatinPIAS1 protein, humanProtein Inhibitors of Activated STATProto-Oncogene Proteins c-mybRNA Polymerase IISmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID21338522
PMCPMC3050860
OpenAlexW2130955459

What OpenQuestion holds

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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.