KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5

Biology

Roberta di Caprio²  Michela Ciano²  Giorgia Montano²  Paola Costanzo¹  Elena Cesaro² 

[1] Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, Italy;

关键词: KRAB-associated protein 1 (KAP1);    protein-protein interaction;    post-translational modifications;    protein arginine methyltransferase;   

DOI  :  10.3390/biology4010041

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.