Evidence map›Paper›PMID 23673342›Full record

ArticleCell cycle (Georgetown, Tex.)2013

SUMO regulates proteasome-dependent degradation of FLASH/Casp8AP2.

Astrid Vennemann, Thomas G Hofmann

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2013. 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
0.7field-weighted citation impact, top 29% 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, 12 citations in OpenAlex.

  1. Review
  2. Article
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  6. Role of the nucleus in apoptosis: signaling and execution.Cellular and molecular life sciences : CMLS · 2015
    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

2 authors at 2 institutions in 1 country.

Astrid VennemannGerman Cancer Research Center (DKFZ), Research Group Cellular Senescence, DKFZ-ZMBH Alliance, Heidelberg, Germany.
Thomas G Hofmann
DKFZ-ZMBH Alliance · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FLASH/Casp8AP2 is a huge multifunctional protein involved in multiple cellular processes, reaching from death receptor signaling to regulation of histone gene transcription and histone mRNA processing. Previous work has shown that FLASH localizes to Cajal bodies and promyelocytic leukemia (PML) bodies. However, the function of its nuclear body association remains unclear. Here we demonstrate that murine FLASH is covalently modified by SUMO at Lys residue 1792. Interestingly, ectopic expression of SUMO results in proteasome-dependent degradation of FLASH. A point mutant of FLASH with a mutated SUMO acceptor lysine residue, FLASH(K1792R), is resistant to SUMO-induced degradation. Finally, we show that arsenic trioxide, a drug known to potentiate SUMO modification and degradation of PML, triggers recruitment of FLASH to PML bodies and concomitant loss of FLASH protein. Our data suggest that SUMO targets FLASH for proteasome-dependent degradation, which is associated with recruitment of FLASH to PML bodies.

Indexed as

AnimalsApoptosis Regulatory ProteinsArsenicalsArsenic TrioxideBiological TransportCalcium-Binding ProteinsCell LineHumansImmunoblottingMiceMicroscopy, ConfocalOxidesProteasome Endopeptidase ComplexSUMO-1 ProteinApoptosis Regulatory ProteinsArsenicalsArsenic TrioxideCalcium-Binding ProteinsCASP8AP2 protein, humanCasp8ap2 protein, mouseOxidesProteasome Endopeptidase ComplexSUMO-1 ProteinFLASH/Casp8AP2proteasome-dependent degradationSUMO

Identifiers

PMID23673342
PMCPMC3735705
OpenAlexW2013942044

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.