Evidence map›Paper›PMID 25585209›Full record

ArticleBiology2015

KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5.

Roberta di Caprio, Michela Ciano, Giorgia Montano, Paola Costanzo, Elena Cesaro

Open access · goldAbstract read
In one paragraph

Article in Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. 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

5 authors at 1 institution in 1 country.

Roberta di CaprioDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy. rob.dicaprio@libero.it.
Michela CianoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy. michelaciano@libero.it.
Giorgia MontanoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy. giorgia.montano@unina.it.
Paola CostanzoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy. paola.costanzo@unina.it.
Elena CesaroDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy. elenacesaro@virgilio.it.
Federico II University Hospital · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

KRAB-associated protein 1 (KAP1), the transcriptional corepressor of Kruppel-associated box zinc finger proteins (KRAB-ZFPs), is subjected to multiple post-translational modifications that are involved in fine-tuning of the multiple biological functions of KAP1. In previous papers, we analyzed the KAP1-dependent molecular mechanism of transcriptional repression mediated by ZNF224, a member of the KRAB-ZFP family, and identified the protein arginine methyltransferase PRMT5 as a component of the ZNF224 repression complex. We demonstrated that PRMT5-mediated histone arginine methylation is required to elicit ZNF224 transcriptional repression. In this study, we show that KAP1 interacts with PRMT5 and is a novel substrate for PRMT5 methylation. Also, we present evidence that the methylation of KAP1 arginine residues regulate the KAP1-ZNF224 interaction, thus suggesting that this KAP1 post-translational modification could actively contribute to the regulation of ZNF224-mediated repression.

Identifiers

PMID25585209
PMCPMC4381216
OpenAlexW1975938433

What OpenQuestion holds

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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.