ДЕФІЦИТ ГЛЮКОЗИ ТА ГЛУТАМІНУ ЗМІНЮЄ ЕКСПРЕСІЮ ГЕНІВ MAP3K5, MAP4K3, CIB1, RIPK1, AND RIPK2 У КЛІТИНАХ ГЛІОМИ ЛІНІЇ U87 З ВИКЛЮЧЕНОЮ ФУНКЦІЄЮ СИГНАЛЬНОГО ЕНЗИМУ ERN1
Анотація
Протеїнкінази відіграють важливу роль у рості злоякісних пухлин як ключові регулятори різноманітних метаболічних процесів. Ми вивчали ефект дефіциту глюкози та глутаміну на рівень експресії мРНК протеїнкінази кінази кінази кінази 3, що активується міогеном, 3 (MAP4K3), протеїнкінази кінази кінази 3, що активується міогеном, 5 (MAP3K5), серин-треонінової кінази 1, що взаємодіє з рецептором TNFRSF (RIPK1), та RIPK2, а також протеїну CIB1, що взаємодіє з протеїнкіназою у клітинах гліоми лінії U87. Встановлено, що пригнічення обох ензиматичних активностей сенсорно-сигнального ензиму ERN1 (сигналювання від ендоплазматичного ретикулуму до ядра-1), основного сенсорно-сигнального ензиму стресу ендоплазматичного ретикулуму, знижує рівень експресії генів, що кодують MAP4K3, RIPK2 та CIB1, але збільшує експресію гена RIPK1. В той же час, не спостерігалось істотних змін в експресії гена MAP3K5 у клітинах гліоми за умов пригнічення сигнального ензиму ERN1. За умов дефіциту глутаміну спостерігалось збільшення рівня експресії гена RIPK1 і зниження – гена CIB1 у контрольних клітинах гліоми, але пригнічення ERN1 модифікувало ефект дефіциту глутаміну на експресію цих генів. Було також показано, що рівень експресії генів MAP3K5, RIPK1, RIPK2 та CIB1 істотно не змінювався у контрольних клітинах гліоми за умов дефіциту глюкози, в той час як у клітинах з пригніченим ERN1 дефіцит глюкози призводив до посилення експресії генів RIPK1 та RIPK2. Таким чином, пригнічення функції ензиму ERN1 також змінює ефект дефіциту глюкози на експресію більшості досліджених генів у клітинах гліоми. Результати цієї роботи чітко вказують на те, що експресія генів MAP4K3, RIPK1, RIPK2 та CIB1 у клітинах гліоми лінії U87 залежить від пригнічення опосередкованого ERN1 стресу ендоплазматичного ретикулуму і переважно змінюється за умов дефіциту глюкози і глутаміну в залежності від функції сигнального ензиму ERN1.
Ключові слова: експресія мРНК, блокада ERN1, MAP3K5, MAP4K3, RIPK1, RIPK2, CIB1, дефіцит глюкози, дефіцит глутаміну, клітини гліоми лінії U87.
Посилання
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Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T. A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis. Oncogene. 2014; 33(9): 1167–1180.
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Denko N.C. Hypoxia, HIF1 and glucose metabolism in the solid tumour. Nature Reviews Cancer. 2008; 8: 705–713.
Drogat B., Auguste P., Nguyen D.T., Bouchecareilh M., Pineau R., Nalbantoglu J., Kaufman R.J., Chevet E., Bikfalvi A., Moenner M. IRE1 signaling is essential for ischemia-induced vascular endothelial growth factor-A expression and contributes to angiogenesis and tumor growth in vivo. Cancer Res. 2007; 67: 6700–6707.
Fels D.R., Koumenis C. The PERK/eIF2a/ATF4 module of the UPR in hypoxia resistance and tumor growth. Cancer Biology & Therapy. 2006; 5(7): 723–728.
Fu Z., Deng B., Liao Y., Shan L., Yin F., Wang Z., Zeng H., Zuo D., Hua Y., Cai Z. The anti-tumor effect of shikonin on osteosarcoma by inducing RIP1 and RIP3 dependent necroptosis. BMC Cancer. 2013; 13: 580.
Hetz C., Chevet E., Harding H.P. Targeting the unfolded protein response in disease. Nat. Rev. Drug Discov. 2013; 12(9): 703–719.
Hollien J., Lin J.H., Li H., Stevens N., Walter P., Weissman J.S. Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J. Cell. Biol. 2009; 186(3): 323–331.
Hayakawa Y., Hirata Y., Nakagawa H., Sakamoto K., Hikiba Y., Kinoshita H., Nakata W., Takahashi R., Tateishi K., Tada M., Akanuma M., Yoshida H., Takeda K., Ichijo H., Omata M., Maeda S., Koike K. Apoptosis signal-regulating kinase 1 and cyclin D1 compose a positive feedback loop contributing to tumor growth in gastric cancer. Proc. Natl. Acad. Sci. U.S.A. 2011; 108(2): 780–785.
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Huang C., Luo Y., Zhao J., Yang F., Zhao H., Fan W., Ge P. Shikonin kills glioma cells through necroptosis mediated by RIP-1. PLoS ONE. 2013; 8(6): E66326.
Ikner A., Ashkenazi A. TWEAK induces apoptosis through a death-signaling complex comprising receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD), and caspase-8. J. Biol. Chem. 286(24): 21546 – 21554.
Johnson A. B., Denko N., Barton M. C. Hypoxia induces a novel signature of chromatin modifications and global repression of transcription. Mutat. Res. 2008; 640: 174–179.
Korennykh A.V., Egea P.F., Korostelev A.A., Finer-Moore J., Zhang C., Shokat K.M., Stroud R.M., Walter P. The unfolded protein response signals through high-order assembly of Ire1. Nature. 2009; 457(7230): 687–693.
Lam D., Dickens D., Reid E.B., Loh S.H., Moisoi N., Martins L.M. MAP4K3 modulates cell death via the post-transcriptional regulation of BH3-only proteins. Proc. Natl. Acad. Sci. U.S.A. 2009; 106(29): 11978–11983.
Lee J., Sun C., Zhou Y., Lee J., Gokalp D., Herrema H., Park S.W., Davis R.J., Ozcan U. p38 MAPK-mediated regulation of Xbp1s is crucial for glucose homeostasis. Nature Medicine. 2011; 17(10): 1251–1260.
Leisner T.M., Moran C., Holly S.P., Parise L.V. CIB1 prevents nuclear GAPDH accumulation and non-apoptotic tumor cell death via AKT and ERK signaling. Oncogene. 2013; 32(34): 4017–4027.
Lenihan C.R., Taylor C.T. The impact of hypoxia on cell death pathways. Biochem. Soc. Trans. 2013; 41(2): 657–663.
Matsuda I., Matsuo K., Matsushita Y., Haruna Y., Niwa M., Kataoka T. The C-terminal domain of the long form of cellular FLICE-inhibitory protein (c-FLIPL) inhibits the interaction of the caspase 8 prodomain with the receptor-interacting protein 1 (RIP1) death domain and regulates caspase 8-dependent nuclear factor kappaB (NF-kappaB) activation. J. Biol. Chem. 2014; 289(7): 3876–3887.
Minchenko D.O., Hubenya O.V., Terletsky B.M., Moenner M., Minchenko O.H. Effect of hypoxia, glutamine and glucose deprivation on the expression of cyclin and cyclin-dependent kinase genes in glioma cell line U87 and its subline with suppressed activity of signaling enzyme endoplasmic reticulum-nuclei-1. Ukr. Biokhim. Zh. 2011; 83(1): 18-29.
Minchenko D.O., Karbovskyi L.L., Danilovskyi S.V., Kharkova A.P., Minchenko O.H. Expression of casein kinase genes in glioma cell line U87: effect of hypoxia and glucose or glutamine deprivation. Nat. Sci. 2012a; 4(1): 38–46.
Minchenko D.O., Minchenko O.H. SNF1/AMP-activated protein kinases: genes, expression and biological role. In: Protein Kinases. Book 1, Dr. Gabriela Da Silva Xavier (Ed.). InTech. 2012b; 41–62.
Minchenko O.H., Kharkova A.P., Bakalets T.V., Kryvdiuk I.V. Endoplasmic reticulum stress, its sensor and signaling systems and the role in the regulation of gene expressions in malignant tumor growth and hypoxia. Ukr. Biochim. J. 2013; 85(5): 5–16.
Minchenko O.H., Kubaichuk K.I., Minchenko D.O., Kovalevska O.V., Kulinich A.O., Lypova N.M. Molecular mechanisms of ERN1-mediated angiogenesis. Int. J. Physiol. Pathophysiol. 2014; 5(1): 1–22.
Moenner M., Pluquet O., Bouchecareilh M., Chevet E. Integrated endoplasmic reticulum stress responses in cancer. Cancer Res. 2007; 67(22): 10631–10634.
Naik M.U., Naik U.P. Calcium- and integrin-binding protein 1 regulates microtubule organization and centrosome segregation through polo like kinase 3 during cell cycle progression. Int. J. Biochem. Cell Biol. 2011; 43(1): 120–129.
Naik M.U., Pham N.T., Beebe K., Dai W., Naik U.P. Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells. Int. J. Cancer. 2011; 128(3): 587–596.
Park S.W., Zhou Y., Lee J., Lu A., Sun C., Chung J., Ueki K., Ozcan U. The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation. Nature Medicine. 2010; 16(4): 429–437.
Pluquet O., Dejeans N., Bouchecareilh M., Lhomond S., Pineau R., Higa A., Delugin M., Combe C., Loriot S., Cubel G., Dugot-Senant N., Vital A., Loiseau H., Gosline S.J., Taouji S., Hallett M., Sarkaria J.N., Anderson K., Wu W., Rodriguez F.J., Rosenbaum J., Saltel F., Fernandez-Zapico M.E., Chevet E. Posttranscriptional regulation of PER1 underlies the oncogenic function of IREα. Cancer Res. 2013; 73(15): 4732–4743.
Rastogi S., Rizwani W., Joshi ,B., Kunigal S., Chellappan S.P. TNF-alpha response of vascular endothelial and vascular smooth muscle cells involve differential utilization of ASK1 kinase and p73. Cell Death Differ. 2012; 19(2): 274–283.
Romero-Ramirez L., Cao H., Nelson D., Hammond E., Lee A.H., Yoshida H., Mori K., Glimcher L.H., Denko N.C., Giaccia A.J., Le Q.-T., Koong A.C. XBP1 is essential for survival under hypoxic conditions and is required for tumor growth. Cancer Res. 2004; 64(17): 5943–5947.
Schriever S.C., Deutsch M.J., Adamski J., Roscher A.A., Ensenauer R. Cellular signaling of amino acids towards mTORC1 activation in impaired human leucine catabolism. J. Nutr. Biochem. 2013; 24(5): 824–831.
Schröder M. Endoplasmic reticulum stress responses. Cell. Mol. Life Sci. 2008; 65(6): 862–894.
Shi Y., Ren Y., Zhao L., Du C., Wang Y., Zhang Y., Li Y., Zhao S., Duan H. Knockdown of thioredoxin interacting protein attenuates high glucose-induced apoptosis and activation of ASK1 in mouse mesangial cells. FEBS Lett. 2011; 585(12): 1789–1795.
Tigno-Aranjuez J.T., Asara J.M., Abbott D.W. Inhibition of RIP2's tyrosine kinase activity limits NOD2-driven cytokine responses. Genes Dev. 2010; 24(23): 2666–2677.
Wang S., Kaufman R.J. The impact of the unfolded protein response on human disease. J. Cell. Biol. 2012; 197(7): 857–867.
Wu S., Kanda T., Nakamoto S., Imazeki F., Yokosuka O. Knockdown of receptor-interacting serine/threonine protein kinase-2 (RIPK2) affects EMT-associated gene expression in human hepatoma cells. Anticancer Res. 2012; 32(9): 3775–3783.
Yan L., Mieulet V., Burgess D., Findlay G.M., Sully K., Procter J., Goris J., Janssens V., Morrice N.A., Lamb R.F. PP2A T61 epsilon is an inhibitor of MAP4K3 in nutrient signaling to mTOR. Mol. Cell. 2010; 37(5): 633–642.
Zhang K., Kaufman R.J. The unfolded protein response: a stress signaling pathway critical for health and disease. Neurology. 2006; 66(2)(Suppl 1): S102–S109.
Zhao B., Han H., Chen J., Zhang Z., Li S., Fang F., Zheng Q., Ma Y., Zhang J., Wu N., Yang Y. MicroRNA let-7c inhibits migration and invasion of human non-small cell lung cancer by targeting ITGB3 and MAP4K3. Cancer Lett. 2014; 342(1): 43–51.
Zhou Y., Lee J., Reno C.M., Sun C., Park S.W., Chung J., Lee J., Fisher S.J., White M.F., Biddinger S.B., Ozcan U. Regulation of glucose homeostasis through a XBP-1-FoxO1 interaction. Nature Medicine. 2011; 17(3): 356–365.
Aragón T., van Anken E., Pincus D., Serafimova I.M., Korennykh A.V., Rubio C.A., Walter P. Messenger RNA targeting to endoplasmic reticulum stress signalling sites. Nature. 2009; 457(7230): 736–740.
Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V., Vandoninck S., Van Lint J., Illing A., Seufferlein T. A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis. Oncogene. 2014; 33(9): 1167–1180.
Auf G., Jabouille A., Delugin M., Guérit S., Pineau R., North S., Platonova N., Maitre M., Favereaux A., Seno M., Bikfalvi A., Minchenko D., Minchenko O., Moenner M. High epiregulin expression in human U87 glioma cells relies on IRE1 and promotes autocrine growth through EGF receptor. BMC Cancer. 2013; 13(1): 597.
Auf G., Jabouille A., Guérit S., Pineau R., Delugin M., Bouchecareilh M., Favereaux A., Maitre M., Gaiser T., von Deimling A., Czabanka M., Vajkoczy P., Chevet E., Bikfalvi A., Moenner M. A shift from an angiogenic to invasive phenotype induced in malignant glioma by inhibition of the unfolded protein response sensor IRE1. Proc. Natl. Acad. Sci. U.S.A. 2010; 107(35): 1555–15558.
Bi M., Naczki C., Koritzinsky M., Fels D., Blais J., Hu N., Harding H., Novoa I., Varia M., Raleigh J., Scheuner D., Kaufman R.J., Bell J., Ron D., Wouters B.G., Koumenis C. ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth. EMBO J. 2005; 24(19): 3470–34815.
Denko N.C. Hypoxia, HIF1 and glucose metabolism in the solid tumour. Nature Reviews Cancer. 2008; 8: 705–713.
Drogat B., Auguste P., Nguyen D.T., Bouchecareilh M., Pineau R., Nalbantoglu J., Kaufman R.J., Chevet E., Bikfalvi A., Moenner M. IRE1 signaling is essential for ischemia-induced vascular endothelial growth factor-A expression and contributes to angiogenesis and tumor growth in vivo. Cancer Res. 2007; 67: 6700–6707.
Fels D.R., Koumenis C. The PERK/eIF2a/ATF4 module of the UPR in hypoxia resistance and tumor growth. Cancer Biology & Therapy. 2006; 5(7): 723–728.
Fu Z., Deng B., Liao Y., Shan L., Yin F., Wang Z., Zeng H., Zuo D., Hua Y., Cai Z. The anti-tumor effect of shikonin on osteosarcoma by inducing RIP1 and RIP3 dependent necroptosis. BMC Cancer. 2013; 13: 580.
Hetz C., Chevet E., Harding H.P. Targeting the unfolded protein response in disease. Nat. Rev. Drug Discov. 2013; 12(9): 703–719.
Hollien J., Lin J.H., Li H., Stevens N., Walter P., Weissman J.S. Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J. Cell. Biol. 2009; 186(3): 323–331.
Hayakawa Y., Hirata Y., Nakagawa H., Sakamoto K., Hikiba Y., Kinoshita H., Nakata W., Takahashi R., Tateishi K., Tada M., Akanuma M., Yoshida H., Takeda K., Ichijo H., Omata M., Maeda S., Koike K. Apoptosis signal-regulating kinase 1 and cyclin D1 compose a positive feedback loop contributing to tumor growth in gastric cancer. Proc. Natl. Acad. Sci. U.S.A. 2011; 108(2): 780–785.
Hong S.W., Shin J.S., Lee Y.M., Kim D.G., Lee S.Y., Yoon D.H., Jung S.Y., Hwang J.J., Lee S.J., Cho D.H., Hong Y.S., Kim T.W., Jin D.H., Lee W.K. p34 (SEI-1) inhibits ROS-induced cell death through suppression of ASK1. Cancer Biol. Ther. 2011; 12(5): 421–426.
Huang C., Luo Y., Zhao J., Yang F., Zhao H., Fan W., Ge P. Shikonin kills glioma cells through necroptosis mediated by RIP-1. PLoS ONE. 2013; 8(6): E66326.
Ikner A., Ashkenazi A. TWEAK induces apoptosis through a death-signaling complex comprising receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD), and caspase-8. J. Biol. Chem. 286(24): 21546 – 21554.
Johnson A. B., Denko N., Barton M. C. Hypoxia induces a novel signature of chromatin modifications and global repression of transcription. Mutat. Res. 2008; 640: 174–179.
Korennykh A.V., Egea P.F., Korostelev A.A., Finer-Moore J., Zhang C., Shokat K.M., Stroud R.M., Walter P. The unfolded protein response signals through high-order assembly of Ire1. Nature. 2009; 457(7230): 687–693.
Lam D., Dickens D., Reid E.B., Loh S.H., Moisoi N., Martins L.M. MAP4K3 modulates cell death via the post-transcriptional regulation of BH3-only proteins. Proc. Natl. Acad. Sci. U.S.A. 2009; 106(29): 11978–11983.
Lee J., Sun C., Zhou Y., Lee J., Gokalp D., Herrema H., Park S.W., Davis R.J., Ozcan U. p38 MAPK-mediated regulation of Xbp1s is crucial for glucose homeostasis. Nature Medicine. 2011; 17(10): 1251–1260.
Leisner T.M., Moran C., Holly S.P., Parise L.V. CIB1 prevents nuclear GAPDH accumulation and non-apoptotic tumor cell death via AKT and ERK signaling. Oncogene. 2013; 32(34): 4017–4027.
Lenihan C.R., Taylor C.T. The impact of hypoxia on cell death pathways. Biochem. Soc. Trans. 2013; 41(2): 657–663.
Matsuda I., Matsuo K., Matsushita Y., Haruna Y., Niwa M., Kataoka T. The C-terminal domain of the long form of cellular FLICE-inhibitory protein (c-FLIPL) inhibits the interaction of the caspase 8 prodomain with the receptor-interacting protein 1 (RIP1) death domain and regulates caspase 8-dependent nuclear factor kappaB (NF-kappaB) activation. J. Biol. Chem. 2014; 289(7): 3876–3887.
Minchenko D.O., Hubenya O.V., Terletsky B.M., Moenner M., Minchenko O.H. Effect of hypoxia, glutamine and glucose deprivation on the expression of cyclin and cyclin-dependent kinase genes in glioma cell line U87 and its subline with suppressed activity of signaling enzyme endoplasmic reticulum-nuclei-1. Ukr. Biokhim. Zh. 2011; 83(1): 18-29.
Minchenko D.O., Karbovskyi L.L., Danilovskyi S.V., Kharkova A.P., Minchenko O.H. Expression of casein kinase genes in glioma cell line U87: effect of hypoxia and glucose or glutamine deprivation. Nat. Sci. 2012a; 4(1): 38–46.
Minchenko D.O., Minchenko O.H. SNF1/AMP-activated protein kinases: genes, expression and biological role. In: Protein Kinases. Book 1, Dr. Gabriela Da Silva Xavier (Ed.). InTech. 2012b; 41–62.
Minchenko O.H., Kharkova A.P., Bakalets T.V., Kryvdiuk I.V. Endoplasmic reticulum stress, its sensor and signaling systems and the role in the regulation of gene expressions in malignant tumor growth and hypoxia. Ukr. Biochim. J. 2013; 85(5): 5–16.
Minchenko O.H., Kubaichuk K.I., Minchenko D.O., Kovalevska O.V., Kulinich A.O., Lypova N.M. Molecular mechanisms of ERN1-mediated angiogenesis. Int. J. Physiol. Pathophysiol. 2014; 5(1): 1–22.
Moenner M., Pluquet O., Bouchecareilh M., Chevet E. Integrated endoplasmic reticulum stress responses in cancer. Cancer Res. 2007; 67(22): 10631–10634.
Naik M.U., Naik U.P. Calcium- and integrin-binding protein 1 regulates microtubule organization and centrosome segregation through polo like kinase 3 during cell cycle progression. Int. J. Biochem. Cell Biol. 2011; 43(1): 120–129.
Naik M.U., Pham N.T., Beebe K., Dai W., Naik U.P. Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells. Int. J. Cancer. 2011; 128(3): 587–596.
Park S.W., Zhou Y., Lee J., Lu A., Sun C., Chung J., Ueki K., Ozcan U. The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation. Nature Medicine. 2010; 16(4): 429–437.
Pluquet O., Dejeans N., Bouchecareilh M., Lhomond S., Pineau R., Higa A., Delugin M., Combe C., Loriot S., Cubel G., Dugot-Senant N., Vital A., Loiseau H., Gosline S.J., Taouji S., Hallett M., Sarkaria J.N., Anderson K., Wu W., Rodriguez F.J., Rosenbaum J., Saltel F., Fernandez-Zapico M.E., Chevet E. Posttranscriptional regulation of PER1 underlies the oncogenic function of IREα. Cancer Res. 2013; 73(15): 4732–4743.
Rastogi S., Rizwani W., Joshi ,B., Kunigal S., Chellappan S.P. TNF-alpha response of vascular endothelial and vascular smooth muscle cells involve differential utilization of ASK1 kinase and p73. Cell Death Differ. 2012; 19(2): 274–283.
Romero-Ramirez L., Cao H., Nelson D., Hammond E., Lee A.H., Yoshida H., Mori K., Glimcher L.H., Denko N.C., Giaccia A.J., Le Q.-T., Koong A.C. XBP1 is essential for survival under hypoxic conditions and is required for tumor growth. Cancer Res. 2004; 64(17): 5943–5947.
Schriever S.C., Deutsch M.J., Adamski J., Roscher A.A., Ensenauer R. Cellular signaling of amino acids towards mTORC1 activation in impaired human leucine catabolism. J. Nutr. Biochem. 2013; 24(5): 824–831.
Schröder M. Endoplasmic reticulum stress responses. Cell. Mol. Life Sci. 2008; 65(6): 862–894.
Shi Y., Ren Y., Zhao L., Du C., Wang Y., Zhang Y., Li Y., Zhao S., Duan H. Knockdown of thioredoxin interacting protein attenuates high glucose-induced apoptosis and activation of ASK1 in mouse mesangial cells. FEBS Lett. 2011; 585(12): 1789–1795.
Tigno-Aranjuez J.T., Asara J.M., Abbott D.W. Inhibition of RIP2's tyrosine kinase activity limits NOD2-driven cytokine responses. Genes Dev. 2010; 24(23): 2666–2677.
Wang S., Kaufman R.J. The impact of the unfolded protein response on human disease. J. Cell. Biol. 2012; 197(7): 857–867.
Wu S., Kanda T., Nakamoto S., Imazeki F., Yokosuka O. Knockdown of receptor-interacting serine/threonine protein kinase-2 (RIPK2) affects EMT-associated gene expression in human hepatoma cells. Anticancer Res. 2012; 32(9): 3775–3783.
Yan L., Mieulet V., Burgess D., Findlay G.M., Sully K., Procter J., Goris J., Janssens V., Morrice N.A., Lamb R.F. PP2A T61 epsilon is an inhibitor of MAP4K3 in nutrient signaling to mTOR. Mol. Cell. 2010; 37(5): 633–642.
Zhang K., Kaufman R.J. The unfolded protein response: a stress signaling pathway critical for health and disease. Neurology. 2006; 66(2)(Suppl 1): S102–S109.
Zhao B., Han H., Chen J., Zhang Z., Li S., Fang F., Zheng Q., Ma Y., Zhang J., Wu N., Yang Y. MicroRNA let-7c inhibits migration and invasion of human non-small cell lung cancer by targeting ITGB3 and MAP4K3. Cancer Lett. 2014; 342(1): 43–51.
Zhou Y., Lee J., Reno C.M., Sun C., Park S.W., Chung J., Lee J., Fisher S.J., White M.F., Biddinger S.B., Ozcan U. Regulation of glucose homeostasis through a XBP-1-FoxO1 interaction. Nature Medicine. 2011; 17(3): 356–365.
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2014-12-31
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БІОХІМІЯ, БІОТЕХНОЛОГІЯ, МОЛЕКУЛЯРНА ГЕНЕТИКА
