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E3 ubiquitin-protein ligase UHRF2

Definition:

E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair. Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them. This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest. Ubiquitinates also PCNP leading to its degradation by the proteasome. Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteosomal degradation. Promotes also DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation. Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation.

References:

[1]. Shunsuke Hanaki, et al. UV-induced activation of ATR is mediated by UHRF2. Genes Cells. 2021 Jun;26(6):447-454. [Content Brief]

[2]. Yuanyuan Li, et al. NIRF induces G1 arrest and associates with Cdk2. Biochem Biophys Res Commun. 2004 Jun 25;319(2):464-8. [Content Brief]

[3]. Ting Zhou, et al. Structural basis for hydroxymethylcytosine recognition by the SRA domain of UHRF2. Mol Cell. 2014 Jun 5;54(5):879-86. [Content Brief]

[4]. Anna Motnenko, et al. Identification of UHRF2 as a novel DNA interstrand crosslink sensor protein. PLoS Genet. 2018 Oct 18;14(10):e1007643. [Content Brief]

[5]. Yangyang Wang, et al. UHRF2 promotes DNA damage response by decreasing p21 via RING finger domain. Biotechnol Lett. 2018 Aug;40(8):1181-1188. [Content Brief]

[6]. Motoko Unoki, et al. ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain. Oncogene. 2004 Oct 7;23(46):7601-10. [Content Brief]

[7]. Tsutomu Mori, et al. NIRF, a novel RING finger protein, is involved in cell-cycle regulation. Biochem Biophys Res Commun. 2002 Aug 23;296(3):530-6. [Content Brief]

[8]. Tsutomu Mori, et al. NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor. Cell Cycle. 2011 Oct 1;10(19):3284-99. [Content Brief]

[9]. Tsutomu Mori, et al. NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein. FEBS Lett. 2004 Jan 16;557(1-3):209-14. [Content Brief]

[10]. Yohan Oh, et al. UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131. J Biol Chem. 2013 Mar 29;288(13):9102-11. [Content Brief]

[11]. Shengyuan Zeng, et al. E3 ligase UHRF2 stabilizes the acetyltransferase TIP60 and regulates H3K9ac and H3K14ac via RING finger domain. Protein Cell. 2017 Mar;8(3):202-218. [Content Brief]

[12]. Robert M Vaughan, et al. Comparative biochemical analysis of UHRF proteins reveals molecular mechanisms that uncouple UHRF2 from DNA methylation maintenance. Nucleic Acids Res. 2018 May 18;46(9):4405-4416. [Content Brief]

[13]. Yidan Liu, et al. Zinc Finger Protein 618 Regulates the Function of UHRF2 (Ubiquitin-like with PHD and Ring Finger Domains 2) as a Specific 5-Hydroxymethylcytosine Reader. J Biol Chem. 2016 Jun 24;291(26):13679-88. [Content Brief]

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