Decrease in MAP3Ks expression enhances the cell death caused by hyperthermia

References

• Roti Roti JL. Cellular responses to hyperthermia (40-46 degrees C): cell killing and molecular events. Int J Hyperthermia. 2008;24(1):3–15.
   PubMed Web of Science ®Google Scholar
• Hou CH, Lin FL, Hou SM, et al. Hyperthermia induces apoptosis through endoplasmic reticulum and reactive oxygen species in human osteosarcoma cells. Int J Mol Sci. 2014;15(10):17380–17395.
   PubMed Web of Science ®Google Scholar
• Ahmed K, Zaidi SF, Mati-Ur-Rehman MR, et al. Hyperthermia and protein homeostasis: cytoprotection and cell death. J Therm Biol. 2020;91:102615.
   PubMed Web of Science ®Google Scholar
• Luo GJ, Sun X, Hasselgren PO. Hyperthermia stimulates energy-proteasome-dependent protein degradation in cultured myotubes. Am J Physiol Regul Integr Comp Physiol. 2000;278(3):R749–R756.
   PubMed Web of Science ®Google Scholar
• Ciechanover A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat Rev Mol Cell Biol. 2005;6(1):79–87.
   PubMed Web of Science ®Google Scholar
• Goll DE, Thompson VF, Li H, et al. The calpain system. Physiol Rev. 2003;83(3):731–801.
   PubMed Web of Science ®Google Scholar
• Song X, Kim SY, Zhou Z, et al. Hyperthermia enhances mapatumumab-induced apoptotic death through ubiquitin-mediated degradation of cellular FLIP(long) in human colon cancer cells. Cell Death Dis. 2013;4(4):e577.
   PubMed Web of Science ®Google Scholar
• van den Tempel N, Odijk H, van Holthe N, et al. Heat-induced BRCA2 degradation in human tumours provides rationale for hyperthermia-PARP-inhibitor combination therapies. Int J Hyperthermia. 2018;34(4):407–414.
   PubMed Web of Science ®Google Scholar
• Chang L, Karin M. Mammalian MAP kinase signalling cascades. Nature. 2001;410(6824):37–40.
   PubMed Web of Science ®Google Scholar
• Cobb MH, Goldsmith EJ. How MAP kinases are regulated. J Biol Chem. 1995;270(25):14843–14846.
   PubMed Web of Science ®Google Scholar
• Yamaguchi K, Shirakabe K, Shibuya H, et al. Identification of a member of the MAPKKK family as a potential mediator of TGF-beta signal transduction. Science. 1995;270(5244):2008–2011.
   PubMed Web of Science ®Google Scholar
• Sakurai H. Targeting of TAK1 in inflammatory disorders and cancer. Trends Pharmacol Sci. 2012;33(10):522–530.
   PubMed Web of Science ®Google Scholar
• Ninomiya-Tsuji J, Kishimoto K, Hiyama A, et al. The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway. Nature. 1999;398(6724):252–256.
   PubMed Web of Science ®Google Scholar
• Leicht DT, Balan V, Kaplun A, et al. Raf kinases: function, regulation and role in human cancer. Biochim Biophys Acta. 2007;1773(8):1196–1212.
   PubMed Web of Science ®Google Scholar
• Mikula M, Schreiber M, Husak Z, et al. Embryonic lethality and fetal liver apoptosis in mice lacking the c-RAF-1 gene. EMBO J. 2001;20(8):1952–1962.
   PubMed Web of Science ®Google Scholar
• Kebache S, Ash J, Annis MG, et al. Grb10 and active RAF-1 kinase promote bad-dependent cell survival. J Biol Chem. 2007;282(30):21873–21883.
   PubMed Web of Science ®Google Scholar
• Blank JL, Gerwins P, Elliott EM, et al. Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. Regulation of sequential phosphorylation pathways involving mitogen-activated protein kinase and c-Jun kinase. J Biol Chem. 1996;271(10):5361–5368.
   PubMed Web of Science ®Google Scholar
• Kesavan K, Lobel-Rice K, Sun W, et al. MEKK2 regulates the coordinate activation of ERK5 and JNK in response to FGF-2 in fibroblasts. J Cell Physiol. 2004;199(1):140–148.
   PubMed Web of Science ®Google Scholar
• Stevenson MA, Calderwood SK, Hahn GM. Effect of hyperthermia (45 °C) on calcium flux in Chinese hamster ovary HA-1 fibroblasts and its potential role in cytotoxicity and heat resistance. Cancer Res. 1987;47(14):3712–3717.
   PubMed Web of Science ®Google Scholar
• Kameda K, Kondo T, Tanabe K, et al. The role of intracellular Ca2+ in apoptosis induced by hyperthermia and its enhancement by verapamil in U937 cells. Int J Radiat Oncol Biol Phys. 2001;49(5):1369–1379.
   PubMed Web of Science ®Google Scholar
• Suzuki K, Hata S, Kawabata Y, et al. Structure, activation, and biology of calpain. Diabetes. 2004;53(1):S12–S18.
   PubMed Web of Science ®Google Scholar
• Moldoveanu T, Hosfield CM, Lim D, et al. A Ca2+ switch aligns the active site of calpain. Cell. 2002;108(5):649–660.
   PubMed Web of Science ®Google Scholar
• Campbell RL, Davies PL. Structure-function relationships in calpains. Biochem J. 2012;447(3):335–351.
   PubMed Web of Science ®Google Scholar
• Enomoto A, Fukasawa T, Tsumoto H, et al. Prevention of calpain-dependent degradation of STK38 by MEKK2-mediated phosphorylation. Sci Rep. 2019;9(1):16010.
   PubMed Web of Science ®Google Scholar
• Cheng J, Yu L, Zhang D, et al. Dimerization through the catalytic domain is essential for MEKK2 activation. J Biol Chem. 2005;280(14):13477–13482.
   PubMed Web of Science ®Google Scholar
• Fan Y, Shi Y, Liu S, et al. Lys48-linked TAK1 polyubiquitination at lysine-72 downregulates TNFα-induced NF-κB activation via mediating TAK1 degradation. Cell Signal. 2012;24(7):1381–1389.
   PubMed Web of Science ®Google Scholar
• Yamashita M, Ying SX, Zhang GM, et al. Ubiquitin ligase smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation. Cell. 2005;121(1):101–113.
   PubMed Web of Science ®Google Scholar
• Cuevas BD, Abell AN, Johnson GL. Role of mitogen-activated protein kinase kinase kinases in signal integration. Oncogene. 2007;26(22):3159–3171.
   PubMed Web of Science ®Google Scholar
• Sato S, Sanjo H, Takeda K, et al. Essential function for the kinase TAK1 in innate and adaptive immune responses. Nat Immunol. 2005;6(11):1087–1095.
   PubMed Web of Science ®Google Scholar
• Takaesu G, Surabhi RM, Park KJ, et al. TAK1 is critical for IkappaB kinase-mediated activation of the NF-kappaB pathway. J Mol Biol. 2003;326(1):105–115.
   PubMed Web of Science ®Google Scholar
• Guo Z, Clydesdale G, Cheng J, et al. Disruption of Mekk2 in mice reveals an unexpected role for MEKK2 in modulating T-cell receptor signal transduction. Mol Cell Biol. 2002;22(16):5761–5768.
   PubMed Web of Science ®Google Scholar
• Garrington TP, Ishizuka T, Papst PJ, et al. MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells. EMBO J. 2000;19(20):5387–5395.
   PubMed Web of Science ®Google Scholar
• Karin M, Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol. 2000;18:621–663.
   PubMed Web of Science ®Google Scholar
• Zhao Q, Lee FS. Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-κB through IκB kinase-alpha and IκB kinase-beta. J Biol Chem. 1999;274(13):8355–8358.
   PubMed Web of Science ®Google Scholar
• Schmidt C, Peng B, Li Z, et al. Mechanisms of proinflammatory cytokine-induced biphasic NF-κB activation. Mol Cell. 2003;12(5):1287–1300.
   PubMed Web of Science ®Google Scholar
• Xia Y, Shen S, Verma IM. NF-κB, an active player in human cancers. Cancer Immunol Res. 2014;2(9):823–830.
   PubMed Web of Science ®Google Scholar
• Furusawa Y, Wei ZL, Sakurai H, et al. TGF-β-activated kinase 1 promotes cell cycle arrest and cell survival of X-ray irradiated HeLa cells dependent on p21 induction but independent of NF-κB, p38 MAPK and ERK phosphorylations. Radiat Res. 2012;177(6):766–774.
   PubMed Web of Science ®Google Scholar
• Tsolou A, Liousia M, Kalamida D, et al. Inhibition of IKK-NFκB pathway sensitizes lung cancer cell lines to radiation. Cancer Biol Med. 2017;14(3):293–301.
   PubMed Web of Science ®Google Scholar
• Broustas CG, Duval AJ, Chaudhary KR, et al. Targeting MEK5 impairs nonhomologous end-joining repair and sensitizes prostate cancer to DNA damaging agents. Oncogene. 2020;39(12):2467–2477.
   PubMed Web of Science ®Google Scholar
• Jiang W, Jin G, Cai F, et al. Extracellular signal-regulated kinase 5 increases radioresistance of lung cancer cells by enhancing the DNA damage response. Exp Mol Med. 2019;51(2):1–20.
   Web of Science ®Google Scholar