JmjC Family of Histone Demethylases Form Nuclear Condensates
The Jumonji-C (JmjC) family of lysine demethylases (KDMs) (JMJC-KDMs) plays an essential role in controlling gene expression and chromatin structure. In most cases, their function has been attributed to the demethylase activity. However, accumulating evidence demonstrates that these proteins play ro...
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| Language: | English |
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MDPI AG
2022-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/14/7664 |
| _version_ | 1797433522785353728 |
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| author | Marta Vicioso-Mantis Samuel Aguirre Marian A. Martínez-Balbás |
| author_facet | Marta Vicioso-Mantis Samuel Aguirre Marian A. Martínez-Balbás |
| author_sort | Marta Vicioso-Mantis |
| collection | DOAJ |
| description | The Jumonji-C (JmjC) family of lysine demethylases (KDMs) (JMJC-KDMs) plays an essential role in controlling gene expression and chromatin structure. In most cases, their function has been attributed to the demethylase activity. However, accumulating evidence demonstrates that these proteins play roles distinct from histone demethylation. This raises the possibility that they might share domains that contribute to their functional outcome. Here, we show that the JMJC-KDMs contain low-complexity domains and intrinsically disordered regions (IDR), which in some cases reached 70% of the protein. Our data revealed that plant homeodomain finger protein (PHF2), KDM2A, and KDM4B cluster by phase separation. Moreover, our molecular analysis implies that PHF2 IDR contributes to transcription regulation. These data suggest that clustering via phase separation is a common feature that JMJC-KDMs utilize to facilitate their functional responses. Our study uncovers a novel potential function for the JMJC-KDM family that sheds light on the mechanisms to achieve the competent concentration of molecules in time and space within the cell nucleus. |
| first_indexed | 2024-03-09T10:18:09Z |
| format | Article |
| id | doaj.art-3f34e2dbe2244ac5b6056d98b50feb4c |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T10:18:09Z |
| publishDate | 2022-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-3f34e2dbe2244ac5b6056d98b50feb4c2023-12-01T22:14:39ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-07-012314766410.3390/ijms23147664JmjC Family of Histone Demethylases Form Nuclear CondensatesMarta Vicioso-Mantis0Samuel Aguirre1Marian A. Martínez-Balbás2Department of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), 08028 Barcelona, SpainDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), 08028 Barcelona, SpainDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), 08028 Barcelona, SpainThe Jumonji-C (JmjC) family of lysine demethylases (KDMs) (JMJC-KDMs) plays an essential role in controlling gene expression and chromatin structure. In most cases, their function has been attributed to the demethylase activity. However, accumulating evidence demonstrates that these proteins play roles distinct from histone demethylation. This raises the possibility that they might share domains that contribute to their functional outcome. Here, we show that the JMJC-KDMs contain low-complexity domains and intrinsically disordered regions (IDR), which in some cases reached 70% of the protein. Our data revealed that plant homeodomain finger protein (PHF2), KDM2A, and KDM4B cluster by phase separation. Moreover, our molecular analysis implies that PHF2 IDR contributes to transcription regulation. These data suggest that clustering via phase separation is a common feature that JMJC-KDMs utilize to facilitate their functional responses. Our study uncovers a novel potential function for the JMJC-KDM family that sheds light on the mechanisms to achieve the competent concentration of molecules in time and space within the cell nucleus.https://www.mdpi.com/1422-0067/23/14/7664epigenetic regulationhistone demethylases (HDM)JmjCIDRphase separation |
| spellingShingle | Marta Vicioso-Mantis Samuel Aguirre Marian A. Martínez-Balbás JmjC Family of Histone Demethylases Form Nuclear Condensates International Journal of Molecular Sciences epigenetic regulation histone demethylases (HDM) JmjC IDR phase separation |
| title | JmjC Family of Histone Demethylases Form Nuclear Condensates |
| title_full | JmjC Family of Histone Demethylases Form Nuclear Condensates |
| title_fullStr | JmjC Family of Histone Demethylases Form Nuclear Condensates |
| title_full_unstemmed | JmjC Family of Histone Demethylases Form Nuclear Condensates |
| title_short | JmjC Family of Histone Demethylases Form Nuclear Condensates |
| title_sort | jmjc family of histone demethylases form nuclear condensates |
| topic | epigenetic regulation histone demethylases (HDM) JmjC IDR phase separation |
| url | https://www.mdpi.com/1422-0067/23/14/7664 |
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