Ubiquitin-protein ligase E3C

Definition

E3 ubiquitin-protein ligase that specifically catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains. Accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Associates with the proteasome and promotes elongation of ubiquitin chains on substrates bound to the 26S proteasome. Also catalyzes 'Lys-29'- and 'Lys-48'-linked ubiquitination of 26S proteasome subunit ADRM1/RPN13 in response to proteotoxic stress, impairing the ability of the proteasome to bind and degrade ubiquitin-conjugated proteins. Acts as a negative regulator of autophagy by mediating 'Lys-29'- and 'Lys-48'-linked ubiquitination of PIK3C3/VPS34, promoting its degradation. Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains; with some preference for 'Lys-48' linkages. Acts as a negative regulator of type I interferon by mediating 'Lys-48'-linked ubiquitination of IRF3 and IRF7, leading to their degradation by the proteasome. Catalyzes ubiquitination and degradation of CAND2.

References:

[1]. J You, et al. A HECT domain E3 enzyme assembles novel polyubiquitin chains. J Biol Chem. 2001 Jun 8;276(23):19871-8. [Content Brief]

[2]. Martin A Michel, et al. Assembly and specific recognition of k29- and k33-linked polyubiquitin. Mol Cell. 2015 Apr 2;58(1):95-109. [Content Brief]

[3]. Min Wang, et al. Molecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase. EMBO J. 2006 Apr 19;25(8):1710-9. [Content Brief]

[4]. Sunil Singh, et al. Crystal structure of HECT domain of UBE3C E3 ligase and its ubiquitination activity. Biochem J. 2020 Mar 13;477(5):905-923. [Content Brief]

[5]. Yuanyuan Yu, et al. K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle. Nat Chem Biol. 2021 Aug;17(8):896-905. [Content Brief]

[6]. Jianxin You, et al. Proteolytic targeting of transcriptional regulator TIP120B by a HECT domain E3 ligase. J Biol Chem. 2003 Jun 27;278(26):23369-75. [Content Brief]

[7]. Min Wang, et al. Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis. EMBO J. 2005 Dec 21;24(24):4324-33. [Content Brief]

[8]. Henrike C Besche, et al. Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates. EMBO J. 2014 May 16;33(10):1159-76. [Content Brief]

[9]. S E Schwarz, et al. Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J Biol Chem. 1998 May 15;273(20):12148-54. [Content Brief]

[10]. Bernard W Chu, et al. The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates. J Biol Chem. 2013 Nov 29;288(48):34575-87. [Content Brief]

[11]. Yu-Hsuan Chen, et al. VPS34 K29/K48 branched ubiquitination governed by UBE3C and TRABID regulates autophagy, proteostasis and liver metabolism. Nat Commun. 2021 Feb 26;12(1):1322. [Content Brief]

[12]. Yanxing Yu, et al. The ubiquitin E3 ligase RAUL negatively regulates type i interferon through ubiquitination of the transcription factors IRF7 and IRF3. Immunity. 2010 Dec 14;33(6):863-77. [Content Brief]

[13]. Yosua Adi Kristariyanto, et al. K29-selective ubiquitin binding domain reveals structural basis of specificity and heterotypic nature of k29 polyubiquitin. Mol Cell. 2015 Apr 2;58(1):83-94. [Content Brief]

[14]. Colin D Gottlieb, et al. Acute unfolding of a single protein immediately stimulates recruitment of ubiquitin protein ligase E3C (UBE3C) to 26S proteasomes. J Biol Chem. 2019 Nov 8;294(45):16511-16524. [Content Brief]

[15]. Chueh-Ling Kuo, et al. Ubiquitinated proteins promote the association of proteasomes with the deubiquitinating enzyme Usp14 and the ubiquitin ligase Ube3c. Proc Natl Acad Sci U S A. 2017 Apr 25;114(17):E3404-E3413. [Content Brief]

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