E3 ubiquitin-protein ligase RING2

Definition:

E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation (By similarity). Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity (Probable). Association with the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes (By similarity). Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation (By similarity).

References:

[1]. Asad M Taherbhoy, et al. BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase. Nat Commun. 2015 Jul 7;6:7621. [Content Brief]

[2]. Hengbin Wang, et al. Role of histone H2A ubiquitination in Polycomb silencing. Nature. 2004 Oct 14;431(7010):873-8. [Content Brief]

[3]. Ru Cao, et al. Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol Cell. 2005 Dec 22;20(6):845-54. [Content Brief]

[4]. Zhonghua Gao, et al. An AUTS2-Polycomb complex activates gene expression in the CNS. Nature. 2014 Dec 18;516(7531):349-54. [Content Brief]

[5]. Zhizhong Li, et al. Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. J Biol Chem. 2006 Jul 21;281(29):20643-9. [Content Brief]

[6]. Robert K McGinty, et al. Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome. Nature. 2014 Oct 30;514(7524):591-6. [Content Brief]

[7]. Renjing Wang, et al. Polycomb group targeting through different binding partners of RING1B C-terminal domain. Structure. 2010 Aug 11;18(8):966-75. [Content Brief]

[8]. Matthew L Bentley, et al. Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. EMBO J. 2011 Jul 19;30(16):3285-97. [Content Brief]

[9]. S J Lee, et al. E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme. FEBS Lett. 2001 Aug 10;503(1):61-4. [Content Brief]

[10]. Xi Luo, et al. Rare deleterious de novo missense variants in Rnf2/Ring2 are associated with a neurodevelopmental disorder with unique clinical features. Hum Mol Genet. 2021 Jun 26;30(14):1283-1292. [Content Brief]

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