Review

Critical function of Siah2 in tumorigenesis

  • Received: 31 July 2017 Accepted: 21 September 2017 Published: 11 October 2017
  • The seven in absentia homolog (Siah) family proteins are components of E3 RING zinc finger ubiquitin ligase complexes that catalyze the ubiquitination of proteins. Siah proteins target their substrates for proteasomal degradation. Evidence is growing that Siah proteins are implicated in the progression of various cancer cells and play a critical role in angiogenesis and tumorigenesis, particularly through Ras, p53, estrogen, and hypoxia inducible factor (HIF)-mediated signaling pathways in response to DNA damage or hypoxia.

    Citation: Kazunobu Baba, Tadaaki Miyazaki. Critical function of Siah2 in tumorigenesis[J]. AIMS Molecular Science, 2017, 4(4): 415-423. doi: 10.3934/molsci.2017.4.415

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  • The seven in absentia homolog (Siah) family proteins are components of E3 RING zinc finger ubiquitin ligase complexes that catalyze the ubiquitination of proteins. Siah proteins target their substrates for proteasomal degradation. Evidence is growing that Siah proteins are implicated in the progression of various cancer cells and play a critical role in angiogenesis and tumorigenesis, particularly through Ras, p53, estrogen, and hypoxia inducible factor (HIF)-mediated signaling pathways in response to DNA damage or hypoxia.


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    [1] Carthew RW, Rubin GM (1990) Seven in absentia, a gene required for specification of R7 cell fate in the Drosophila eye. Cell 63: 561-577. doi: 10.1016/0092-8674(90)90452-K
    [2] Della NG, Senior PV, Bowtell DL (1993) Isolation and characterization of murine homologues of the Drosophila seven in absentia gene (Sina). Development 117: 1333-1343.
    [3] Holloway AJ, Della NG, Fletcher CF, et al. (1997) Chromosomal mapping of five highly conserved murine homologues of the Drosophila RING finger gene seven-in-absentia. Genomics 41: 160-168. doi: 10.1006/geno.1997.4642
    [4] House CM, Hancock NC, Moller A, et al. (2006) Elucidation of the substrate binding site of Siah ubiquitin ligase. Structure 14: 695-701. doi: 10.1016/j.str.2005.12.013
    [5] House CM, Frew IJ, Huang HL, et al. (2003) A binding motif for Siah ubiquitin ligase. Proc Natl Acad Sci USA 100: 3101-3106. doi: 10.1073/pnas.0534783100
    [6] Khurana A, Nakayama K, Williams S, et al. (2006) Regulation of the ring finger E3 ligase Siah2 by p38 MAPK. J Biol Chem 281: 35316-35326. doi: 10.1074/jbc.M606568200
    [7] Scortegagna M, Subtil T, Qi J, et al. (2011) USP13 enzyme regulates Siah2 ligase stability and activity via noncatalytic ubiquitin-binding domains. J Biol Chem 286: 27333-27341. doi: 10.1074/jbc.M111.218214
    [8] Matsuzawa SI, Reed JC (2001) Siah-1, SIP, and Ebi Collaborate in a Novel Pathway for b-Catenin Degradation Linked to p53 Responses. Mol Cell 7: 915-926. doi: 10.1016/S1097-2765(01)00242-8
    [9] Winter M, Sombroek D, Dauth I, et al. (2008) Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR. Nat Cell Biol 10: 812-824. doi: 10.1038/ncb1743
    [10] Zundel W, Schindler C, Haas-Kogan D, et al. (2000) Loss of PTEN facilitates HIF-1-mediated gene expression. Genes Dev 14: 391-396.
    [11] Carthew RW, Neufeld TP, Rubin GM (1994) Identification of genes that interact with the sina gene in Drosophila eye development. Proc Natl Acad Sci USA 91: 11689-11693. doi: 10.1073/pnas.91.24.11689
    [12] Tang AH, Neufeld TP, Kwan E, et al. (1997) PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism. Cell 90: 459-467. doi: 10.1016/S0092-8674(00)80506-1
    [13] Bogdan S, Senkel S, Esser F, et al. (2001) Misexpression of Xsiah-2 induces a small eye phenotype in Xenopus. Mech Dev 103: 61-69.
    [14] Zhang J, Guenther MG, Carthew RW, et al. (1998) Proteasomal regulation of nuclear receptor corepressor-mediated repression. Genes Dev 12: 1775-1780. doi: 10.1101/gad.12.12.1775
    [15] D'Orazi G, Cecchinelli B, Bruno T, et al. (2002) Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis. Nat Cell Biol 4: 11-19. doi: 10.1038/ncb714
    [16] Johnsen SA, Subramaniam M, Monroe DG, et al. (2002) 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 277: 30754-30759. doi: 10.1074/jbc.M204812200
    [17] Hu G, Fearon ER (1999) 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 1: 19724-19732.
    [18] Maxwell PH, Ratciffe PJ (2002) Oxygen sensors and angiogenesis. Semin Cell Dev Biol 13: 29-37. doi: 10.1006/scdb.2001.0287
    [19] McNeill LA, Hewitson KS, Gleadle JM (2002) The use of dioxygen by HIF prolyl hydroxylase (PHD1). Bioorg Med Chem Lett 12: 1547-1550. doi: 10.1016/S0960-894X(02)00219-6
    [20] Qi J, Nakayama K, Gaitonde S, et al. (2008) Siah2-dependent concerted activity of HIF and FoxA2 regulates formation of neuroendocrine phenotype and neuroendocrine prostate tumors. Proc Natl Acad Sci USA 105: 16713-16718. doi: 10.1073/pnas.0804063105
    [21] Baba K, Morimoto H, Imaoka S (2013) Seven in absentia homolog 2 (Siah2) protein is a regulator of NF-E2-related factor 2 (Nrf2). J Biol Chem 288: 18393-18405. doi: 10.1074/jbc.M112.438762
    [22] Sajja RK, Green KN, Cucullo L (2015) Altered Nrf2 signaling mediates hypoglycemia-induced blood-brain barrier endothelial dysfunction in vitro. PLos One 10: e0122358. doi: 10.1371/journal.pone.0122358
    [23] Itoh K, Wakabayashi N, Katoh Y, et al. (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev 13: 76-86. doi: 10.1101/gad.13.1.76
    [24] Kim H, Scimia MC, Wilkinson D (2011) Fine-tuning of Drp1/Fis1 availability by AKAP121/Siah2 regulates mitochondrial adaptation to hypoxia. Mol Cell 44: 532-544 doi: 10.1016/j.molcel.2011.08.045
    [25] Li Q, Wang P, Ye K, et al. (2015) Central role of SIAH inhibition in DCC-dependent cardioprotection provoked by netrin-1/NO. Proc Natl Acad USA 112: 899-904. doi: 10.1073/pnas.1420695112
    [26] Schmidt RL, Park CH, Ahmed AU, et al. (2007) Inhibition of RAS-mediated transformation and tumorigenesis by targeting the downstream E3 ubiquitin ligase seven in absentia homologue. Cancer Res 67: 11798-11810. doi: 10.1158/0008-5472.CAN-06-4471
    [27] Kim CJ, Cho YG, Park CH, et al. (2004) Inactivating mutations of the Siah-1 gene in gastric cancer. Oncogene 23: 8591-8596. doi: 10.1038/sj.onc.1208113
    [28] Ahmed AU, Sxhmidt RL, Park CH, et al. (2008) Effect of disrupting seven-in-absentia homolog 2 function on lung cancer cell growth. J Natl Cancer Inst 100: 1606-29. doi: 10.1093/jnci/djn365
    [29] Wong CS, Sceneay J, House CM, et al. (2012) Vascular normalization by loss of Siah2 results an increased chemotherapeutic efficacy. Cancer Res 72: 1694-1704. doi: 10.1158/0008-5472.CAN-11-3310
    [30] Shah M, Stebbins JL, Dewing A, et al. (2009) Inhibition of Siah2 ubiquitin ligase by vitamin K3 (menadione) attenuates hypoxia and MAPK signaling and blocks melanoma tumorigenesis. Pigment Cell Melanoma Res 22: 799-808. doi: 10.1111/j.1755-148X.2009.00628.x
    [31] Qi J, Nakayama K, Cardiff RD, et al. (2010) Siah2-dependent concerted activity of HIF and FoxA2 regulates formation of neuroendocrine phenotype and neuroendocrine prostate tumors. Cancer Cell 18: 23-38. doi: 10.1016/j.ccr.2010.05.024
    [32] Yoshibayashi H, Okabe H, Satoh S, et al. (2007) SIAH1 causes growth arrst and apoptosis in hepatoma cells through beta-catenin degradation-dependent and –independent mechanisms. Oncol Rep 17: 549-556.
    [33] Roperch J, Lethrone F, Prieur S, et al. (1999) SIAH-1 promotes apoptosis and tumor suppression through a network involving the regulation of protein folding, unfolding, and trafficking: identification of common effectors with p53 and p21(Waf1). Proc Natl Acad USA 96: 8070-8073. doi: 10.1073/pnas.96.14.8070
    [34] Malz M, Aulmann A, Samarin J, et al. (2012) Nuclear accumulation of seven in absentia homologue-2 supports motility and proliferation of liver cancer cells. Int J Cancer 131: 2016-2026. doi: 10.1002/ijc.27473
    [35] Wong CS, Moller A (2013) Siah: a promising anticancer target. Cancer Res 73: 2400-2406. doi: 10.1158/0008-5472.CAN-12-4348
    [36] DeBruyne JP, Baggs JE, Sato TK (2015) Ubiquitin ligase Siah2 regulates RevErba degradation and the mammalian circadian clock. Proc Natl Acad Sci USA 112: 12420-12425. doi: 10.1073/pnas.1501204112
    [37] Adam MG, Matt S, Christian S (2015) SIAH ubiquitin ligases regulate breast cancer cell migration and invasion independent of the oxygen status. Cell Cycle 14: 3734-3747. doi: 10.1080/15384101.2015.1104441
    [38] Frasor J, Danes JM, Funk CC, et al. (2005) Estrogen down-regulation of the corepressor N-CoR: mechanism and implications for estrogen derepression of N-CoR-regulated genes. Proc Natl Acad Sci USA 102: 13153-13157. doi: 10.1073/pnas.0502782102
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