E3 ubiquitin-protein ligase synoviolin

Definition:

E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis. Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (By similarity). During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells (By similarity).

References:

[1]. Tetsuya Amano, et al. Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy. Genes Dev. 2003 Oct 1;17(19):2436-49. [Content Brief]

[2]. Tomohiro Omura, et al. A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin. J Neurochem. 2006 Dec;99(6):1456-69. [Content Brief]

[3]. Masayuki Kaneko, et al. Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation. FEBS Lett. 2002 Dec 4;532(1-2):147-52. [Content Brief]

[4]. Nobuko Hosokawa, et al. Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-L. FEBS J. 2016 Jan;283(1):157-72. [Content Brief]

[5]. Takashi Sato, et al. STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein. Mol Cell. 2012 Jul 13;47(1):99-110. [Content Brief]

[6]. Eran Nadav, et al. A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1. Biochem Biophys Res Commun. 2003 Mar 28;303(1):91-7. [Content Brief]

[7]. Satoshi Yamasaki, et al. Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'. EMBO J. 2007 Jan 10;26(1):113-22. [Content Brief]

[8]. Wen-Fang Wang, et al. HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells. Nat Commun. 2017 Aug 25;8(1):363. [Content Brief]

[9]. Hui Yang, et al. Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin. Exp Cell Res. 2007 Feb 1;313(3):538-50. [Content Brief]

[10]. Marjolein Kikkert, et al. Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J Biol Chem. 2004 Jan 30;279(5):3525-34. [Content Brief]

[11]. Jasmin Schulz, et al. Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD). J Cell Sci. 2017 Oct 1;130(19):3322-3335. [Content Brief]

[12]. Andrea Schulze, et al. The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. J Mol Biol. 2005 Dec 16;354(5):1021-7. [Content Brief]

[13]. Maria Francisca Arteaga, et al. An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery. Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11178-83. [Content Brief]

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