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Seven in absentia homolog 2

Siah2, Siaz
This gene encodes a protein that is a member of the seven in absentia homolog (SIAH) family. The protein is an E3 ligase and is involved in ubiquitination and proteasome-mediated degradation of specific proteins. The activity of this ubiquitin ligase has been implicated in regulating cellular response to hypoxia. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, Siah-1, V1a, CAN, p53
Papers on Siah2
CHK2 stability is regulated by the E3 ubiquitin ligase SIAH2.
Calzado et al., Córdoba, Spain. In Oncogene, Feb 2016
In the present study, we identify the ubiquitin E3 ligase SIAH2 as an interaction partner of CHK2, which mediates its ubiquitination and proteasomal degradation.
Overexpression of Siah2 Is Associated With Poor Prognosis in Patients With Epithelial Ovarian Carcinoma.
Chen et al., Harbin, China. In Int J Gynecol Cancer, Jan 2016
OBJECTIVES: Seven in absentia homolog 2 (Siah2) is an E3 ubiquitin ligase that is expressed in mammals and is homologous to seven in absentia in Drosophila.
SIAH ubiquitin ligases regulate breast cancer cell migration and invasion independent of the oxygen status.
Algire et al., Heidelberg, Germany. In Cell Cycle, Jan 2016
Many studies suggest a tumorigenic role for SIAH2.
Ubiquitin ligase Siah2 regulates RevErbα degradation and the mammalian circadian clock.
Hogenesch et al., Philadelphia, United States. In Proc Natl Acad Sci U S A, Nov 2015
We screened the nuclear hormone receptor RevErbα (Nr1d1), a key constituent of the mammalian circadian clock, for E3 ligases that regulate its stability and found Seven in absentia2 (Siah2) to be a key regulator of RevErbα stability.
The inducible E3 ubiquitin ligases SIAH1 and SIAH2 perform critical roles in breast and prostate cancers.
Krämer et al., Essen, Germany. In Cytokine Growth Factor Rev, Aug 2015
An increasing body of evidence suggests that the E3 ubiquitin ligases SIAH1 and SIAH2 are able to dictate the growth, development, and chemo-/radiosensitivity of breast and prostate cancer cells.
Hypoxia regulates Hippo signalling through the SIAH2 ubiquitin E3 ligase.
Wu et al., Tianjin, China. In Nat Cell Biol, 2015
We demonstrate that the E3 ubiquitin ligase SIAH2 stimulates YAP by destabilizing LATS2, a critical component of the Hippo pathway, in response to hypoxia.
The Expression of the Ubiquitin Ligase SIAH2 (Seven In Absentia Homolog 2) Is Increased in Human Lung Cancer.
Calzado et al., Córdoba, Spain. In Plos One, 2014
The aim of the study was to document SIAH2 expression pattern at different levels (mRNA, protein level and immunohistochemistry) in human non-small cell lung cancer (NSCLC) samples compared to surrounding healthy tissue from the same patient, and to analyse the association with clinicopathological features.
Hypoxic regulation of glutamine metabolism through HIF1 and SIAH2 supports lipid synthesis that is necessary for tumor growth.
Denko et al., Columbus, United States. In Cell Metab, 2014
HIF-1 activation promotes SIAH2 targeted ubiquitination and proteolysis of the 48 kDa splice variant of the E1 subunit of the αKGDH complex (OGDH2).
SIAH proteins: critical roles in leukemogenesis.
Knauer et al., Jena, Germany. In Leukemia, 2013
Here, we summarize functions of SIAH ubiquitin-ligases in leukemias, how they select leukemia-relevant substrates for proteasomal degradation, and how the expression and activity of SIAH1 and SIAH2 can be modulated in vivo.
The E3 ubiquitin ligase Siah2 contributes to castration-resistant prostate cancer by regulation of androgen receptor transcriptional activity.
Ronai et al., Los Angeles, United States. In Cancer Cell, 2013
We demonstrate that the ubiquitin ligase Siah2 targets a select pool of NCOR1-bound, transcriptionally-inactive AR for ubiquitin-dependent degradation, thereby promoting expression of select AR target genes implicated in lipid metabolism, cell motility, and proliferation.
Nuclear accumulation of seven in absentia homologue-2 supports motility and proliferation of liver cancer cells.
Breuhahn et al., Heidelberg, Germany. In Int J Cancer, 2012
SIAH-2 - as described for SIAH-1 - accumulates in nuclei of hepatocellular carcinoma cells where it supports tumor growth and tumor cell dissemination
Vascular normalization by loss of Siah2 results in increased chemotherapeutic efficacy.
Möller et al., Melbourne, Australia. In Cancer Res, 2012
Blood vessel normalization in Siah2(-/-) tumors resulted in an increased response to chemotherapy and prolonged survival
The ubiquitin ligase Siah2 regulates PPARγ activity in adipocytes.
Floyd et al., Baton Rouge, United States. In Endocrinology, 2012
modulation of PPARgamma protein levels by the ubiquitin ligase Siah2 is essential in determining the physiological effects of PPARgamma activation in adipocytes
TIN2 stability is regulated by the E3 ligase Siah2.
Smith et al., New York City, United States. In Mol Cell Biol, 2012
Siah2 acts as an E3 ligase to directly ubiquitylate TIN2 in vitro.
Fine-tuning of Drp1/Fis1 availability by AKAP121/Siah2 regulates mitochondrial adaptation to hypoxia.
Ronai et al., Los Angeles, United States. In Mol Cell, 2011
Siah2 is a key regulator of hypoxia-induced mitochondrial fission and plays role in ischemic injury
The Siah2-HIF-FoxA2 axis in prostate cancer – new markers and therapeutic opportunities.
Ronai et al., Los Angeles, United States. In Oncotarget, 2010
Review: Define the regulatory axis consisting of Siah2 and HIF-1alpha/FoxA2 cooperation and suggest novel therapeutic modalities to treat these most aggressive forms of prostate cancer.
Siah2-dependent concerted activity of HIF and FoxA2 regulates formation of neuroendocrine phenotype and neuroendocrine prostate tumors.
Ronai et al., Los Angeles, United States. In Cancer Cell, 2010
Siah2-dependent concerted activity of HIF and FoxA2 regulates formation of neuroendocrine phenotype and neuroendocrine prostate tumors.
Sprouty proteins: modified modulators, matchmakers or missing links?
Chow et al., Singapore, Singapore. In J Endocrinol, 2009
Significantly, two ubiquitin E3 ligases also bind to the N-terminus of Sprouty: c-Cbl binds with high affinity to the TKB binding motif and SIAH2 binds constitutively to a different site; both proteins are able to direct the ubiquitination of Sprouty proteins and its destruction.
The ubiquitin ligase Siah2 and the hypoxia response.
Ronai et al., Los Angeles, United States. In Mol Cancer Res, 2009
Among them, Siah2, a RING finger ligase, is an important regulator of pathways activated under hypoxia.
An inducible autoregulatory loop between HIPK2 and Siah2 at the apex of the hypoxic response.
Schmitz et al., Gießen, Germany. In Nat Cell Biol, 2009
Hypoxic conditions allow a markedly increased HIPK2/Siah2 interaction and result in efficient polyubiquitylation and proteasomal degradation of the kinase.
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