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000126010 0247_ $$2doi$$a10.1080/15384101.2015.1104441
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000126010 0247_ $$2ISSN$$a1551-4005
000126010 037__ $$aDKFZ-2017-02125
000126010 041__ $$aeng
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000126010 1001_ $$0P:(DE-HGF)0$$aAdam, M Gordian$$b0$$eFirst author
000126010 245__ $$aSIAH ubiquitin ligases regulate breast cancer cell migration and invasion independent of the oxygen status.
000126010 260__ $$aGeorgetown, Tex.$$bLandes Bioscience$$c2015
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000126010 520__ $$aSeven-in-absentia homolog (SIAH) proteins are evolutionary conserved RING type E3 ubiquitin ligases responsible for the degradation of key molecules regulating DNA damage response, hypoxic adaptation, apoptosis, angiogenesis, and cell proliferation. Many studies suggest a tumorigenic role for SIAH2. In breast cancer patients SIAH2 expression levels correlate with cancer aggressiveness and overall patient survival. In addition, SIAH inhibition reduced metastasis in melanoma. The role of SIAH1 in breast cancer is still ambiguous; both tumorigenic and tumor suppressive functions have been reported. Other studies categorized SIAH ligases as either pro- or antimigratory, while the significance for metastasis is largely unknown. Here, we re-evaluated the effects of SIAH1 and SIAH2 depletion in breast cancer cell lines, focusing on migration and invasion. We successfully knocked down SIAH1 and SIAH2 in several breast cancer cell lines. In luminal type MCF7 cells, this led to stabilization of the SIAH substrate Prolyl Hydroxylase Domain protein 3 (PHD3) and reduced Hypoxia-Inducible Factor 1α (HIF1α) protein levels. Both the knockdown of SIAH1 or SIAH2 led to increased apoptosis and reduced proliferation, with comparable effects. These results point to a tumor promoting role for SIAH1 in breast cancer similar to SIAH2. In addition, depletion of SIAH1 or SIAH2 also led to decreased cell migration and invasion in breast cancer cells. SIAH knockdown also controlled microtubule dynamics by markedly decreasing the protein levels of stathmin, most likely via p27(Kip1). Collectively, these results suggest that both SIAH ligases promote a migratory cancer cell phenotype and could contribute to metastasis in breast cancer.
000126010 536__ $$0G:(DE-HGF)POF3-311$$a311 - Signalling pathways, cell and tumor biology (POF3-311)$$cPOF3-311$$fPOF III$$x0
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000126010 650_7 $$2NLM Chemicals$$aCDKN1B protein, human
000126010 650_7 $$2NLM Chemicals$$aNuclear Proteins
000126010 650_7 $$2NLM Chemicals$$aStathmin
000126010 650_7 $$0147604-94-2$$2NLM Chemicals$$aCyclin-Dependent Kinase Inhibitor p27
000126010 650_7 $$0EC 2.3.2.27$$2NLM Chemicals$$aUbiquitin-Protein Ligases
000126010 650_7 $$0EC 2.3.2.27$$2NLM Chemicals$$aseven in absentia proteins
000126010 7001_ $$0P:(DE-HGF)0$$aMatt, Sonja$$b1
000126010 7001_ $$aChristian, Sven$$b2
000126010 7001_ $$aHess-Stumpp, Holger$$b3
000126010 7001_ $$aHaegebarth, Andrea$$b4
000126010 7001_ $$0P:(DE-He78)99ae95278bd95e30462a4fb2d12026c6$$aHofmann, Thomas$$b5$$udkfz
000126010 7001_ $$aAlgire, Carolyn$$b6
000126010 773__ $$0PERI:(DE-600)2102687-7$$a10.1080/15384101.2015.1104441$$gVol. 14, no. 23, p. 3734 - 3747$$n23$$p3734 - 3747$$tCell cycle$$v14$$x1551-4005$$y2015
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000126010 9141_ $$y2015
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