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E3 ubiquitin-protein ligase SIAH1

Definition:

E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation. It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling. Has some overlapping function with SIAH2. Induces apoptosis in cooperation with PEG3 (By similarity). Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus (By similarity). GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins (By similarity). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1.

References:

[1]. Mirco Fanelli, et al. The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome. J Biol Chem. 2004 Feb 13;279(7):5374-9. [Content Brief]

[2]. J Boehm, et al. Regulation of BOB.1/OBF.1 stability by SIAH. EMBO J. 2001 Aug 1;20(15):4153-62. [Content Brief]

[3]. L Susini, et al. Siah-1 binds and regulates the function of Numb. Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15067-72. [Content Brief]

[4]. Yoshito Nagano, et al. Siah-1 facilitates ubiquitination and degradation of synphilin-1. J Biol Chem. 2003 Dec 19;278(51):51504-14. [Content Brief]

[5]. Magdalena C Liebl, et al. DAZAP2 acts as specifier of the p53 response to DNA damage. Nucleic Acids Res. 2021 Mar 18;49(5):2759-2776. [Content Brief]

[6]. G Hu, et al. Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway. Genes Dev. 1997 Oct 15;11(20):2701-14. [Content Brief]

[7]. Antonia Germani, et al. SIAH-1 interacts with CtIP and promotes its degradation by the proteasome pathway. Oncogene. 2003 Dec 4;22(55):8845-51. [Content Brief]

[8]. J Tanikawa, et al. p53 suppresses the c-Myb-induced activation of heat shock transcription factor 3. J Biol Chem. 2000 May 19;275(20):15578-85. [Content Brief]

[9]. R Tiedt, et al. The RING finger protein Siah-1 regulates the level of the transcriptional coactivator OBF-1. EMBO J. 2001 Aug 1;20(15):4143-52. [Content Brief]

[10]. M Buchwald, et al. Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3 for proteasomal degradation. Leukemia. 2010 Aug;24(8):1412-21. [Content Brief]

[11]. Melanie Winter, et al. Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR. Nat Cell Biol. 2008 Jul;10(7):812-24. [Content Brief]

[12]. J Liu, et al. Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein. Mol Cell. 2001 May;7(5):927-36. [Content Brief]

[13]. S I Matsuzawa, et al. Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses. Mol Cell. 2001 May;7(5):915-26. [Content Brief]

[14]. Lei Ji, et al. The SIAH E3 ubiquitin ligases promote Wnt/β-catenin signaling through mediating Wnt-induced Axin degradation. Genes Dev. 2017 May 1;31(9):904-915. [Content Brief]

[15]. A Germani, et al. SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis. Oncogene. 2000 Dec 7;19(52):5997-6006. [Content Brief]

[16]. Min Liu, et al. The ubiquitin ligase Siah1 controls ELL2 stability and formation of super elongation complexes to modulate gene transcription. Mol Cell. 2012 May 11;46(3):325-34. [Content Brief]

[17]. Julien Buratti, et al. De novo variants in SIAH1, encoding an E3 ubiquitin ligase, are associated with developmental delay, hypotonia and dysmorphic features. J Med Genet. 2021 Mar;58(3):205-212. [Content Brief]

[18]. Raymonde Szargel, et al. Synphilin-1A inhibits seven in absentia homolog (SIAH) and modulates alpha-synuclein monoubiquitylation and inclusion formation. J Biol Chem. 2009 Apr 24;284(17):11706-16. [Content Brief]

[19]. G Hu, et al. Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. Mol Cell Biol. 1999 Jan;19(1):724-32. [Content Brief]

[20]. Eugenio Santelli, et al. Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex. J Biol Chem. 2005 Oct 7;280(40):34278-87. [Content Brief]

[21]. Esti Liani, et al. Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease. Proc Natl Acad Sci U S A. 2004 Apr 13;101(15):5500-5. [Content Brief]

[22]. Steven A Johnsen, et al. Modulation of transforming growth factor beta (TGFbeta)/Smad transcriptional responses through targeted degradation of TGFbeta-inducible early gene-1 by human seven in absentia homologue. J Biol Chem. 2002 Aug 23;277(34):30754-9. [Content Brief]

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