Next Article in Journal
Treatment of Leptothrix Cells with Ultrapure Water Poses a Threat to Their Viability
Next Article in Special Issue
PDZ Domain Recognition: Insight from Human Tax-Interacting Protein 1 (TIP-1) Interaction with Target Proteins
Previous Article in Journal
Acknowledgement to Reviewers of Biology in 2014
Article Menu

Export Article

Open AccessCommunication
Biology 2015, 4(1), 41-49; doi:10.3390/biology4010041

KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5

Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy
*
Author to whom correspondence should be addressed.
Academic Editor: Thorsten Berg
Received: 28 November 2014 / Accepted: 4 January 2015 / Published: 9 January 2015
(This article belongs to the Special Issue Protein-Protein Interactions)
View Full-Text   |   Download PDF [306 KB, uploaded 9 January 2015]   |  

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. View Full-Text
Keywords: KRAB-associated protein 1 (KAP1); protein-protein interaction; post-translational modifications; protein arginine methyltransferase KRAB-associated protein 1 (KAP1); protein-protein interaction; post-translational modifications; protein arginine methyltransferase
Figures

Figure 1a

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

di Caprio, R.; Ciano, M.; Montano, G.; Costanzo, P.; Cesaro, E. KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5. Biology 2015, 4, 41-49.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biology EISSN 2079-7737 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top