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.

KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5 / DI CAPRIO, Roberta; Ciano, Michela; Montano, Giorgia; Costanzo, Paola; Cesaro, Elena. - In: BIOLOGY. - ISSN 2079-7737. - 4:1(2015), pp. 41-49. [10.3390/biology4010041]

KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5

DI CAPRIO, ROBERTA;CIANO, MICHELA;MONTANO, GIORGIA;COSTANZO, PAOLA;CESARO, Elena
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.
2015
KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5 / DI CAPRIO, Roberta; Ciano, Michela; Montano, Giorgia; Costanzo, Paola; Cesaro, Elena. - In: BIOLOGY. - ISSN 2079-7737. - 4:1(2015), pp. 41-49. [10.3390/biology4010041]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/677938
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