KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5
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...
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MDPI AG
2015-01-01
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| Series: | Biology |
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| Online Access: | http://www.mdpi.com/2079-7737/4/1/41 |
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| author | Roberta di Caprio Michela Ciano Giorgia Montano Paola Costanzo Elena Cesaro |
| author_facet | Roberta di Caprio Michela Ciano Giorgia Montano Paola Costanzo Elena Cesaro |
| author_sort | Roberta di Caprio |
| collection | DOAJ |
| description | 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. |
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| format | Article |
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| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-12T08:20:54Z |
| publishDate | 2015-01-01 |
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| spelling | doaj.art-9496b98d94924bbebce6c2fca25f7ed32023-09-02T18:31:09ZengMDPI AGBiology2079-77372015-01-0141414910.3390/biology4010041biology4010041KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5Roberta di Caprio0Michela Ciano1Giorgia Montano2Paola Costanzo3Elena Cesaro4Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, ItalyDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, ItalyDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, ItalyDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, ItalyDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, via S. Pansini 5, Naples 80131, ItalyKRAB-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.http://www.mdpi.com/2079-7737/4/1/41KRAB-associated protein 1 (KAP1)protein-protein interactionpost-translational modificationsprotein arginine methyltransferase |
| spellingShingle | Roberta di Caprio Michela Ciano Giorgia Montano Paola Costanzo Elena Cesaro KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5 Biology KRAB-associated protein 1 (KAP1) protein-protein interaction post-translational modifications protein arginine methyltransferase |
| title | KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5 |
| title_full | KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5 |
| title_fullStr | KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5 |
| title_full_unstemmed | KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5 |
| title_short | KAP1 is a Novel Substrate for the Arginine Methyltransferase PRMT5 |
| title_sort | kap1 is a novel substrate for the arginine methyltransferase prmt5 |
| topic | KRAB-associated protein 1 (KAP1) protein-protein interaction post-translational modifications protein arginine methyltransferase |
| url | http://www.mdpi.com/2079-7737/4/1/41 |
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