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
Will Lipidation of ApoA1 through Interaction with ABCA1 at the Intestinal Level Affect the Protective Functions of HDL?
Open AccessCommunication

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
Biology 2015, 4(1), 41-49; https://doi.org/10.3390/biology4010041
Received: 28 November 2014 / Accepted: 4 January 2015 / Published: 9 January 2015
(This article belongs to the Special Issue Protein-Protein Interactions)
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
Show Figures

Figure 1

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

Article Access Map by Country/Region

1
Only visits after 24 November 2015 are recorded.
Back to TopTop