KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5
AbstractKRAB-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
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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.
di Caprio R, Ciano M, Montano G, Costanzo P, Cesaro E. KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5. Biology. 2015; 4(1):41-49.Chicago/Turabian Style
di Caprio, Roberta; Ciano, Michela; Montano, Giorgia; Costanzo, Paola; Cesaro, Elena. 2015. "KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5." Biology 4, no. 1: 41-49.