RIPK1 regulates survival of human melanoma cells upon endoplasmic reticulum stress through autophagy

References

• Festjens N, Vanden Berghe T, Cornelis S, Vandenabeele P. RIP1, a kinase on the crossroads of a cell's decision to live or die. Cell Death Differ 2007; 14:400-10; PMID:17301840; http://dx.doi.org/10.1038/sj.cdd.4402085
   PubMed Web of Science ®Google Scholar
• Wang L, Du F, Wang X. TNF-alpha induces two distinct caspase-8 activation pathways. Cell 2008; 133:693-703; PMID:18485876; http://dx.doi.org/10.1016/j.cell.2008.03.036
   PubMed Web of Science ®Google Scholar
• Christofferson DE, Li Y, Hitomi J, Zhou W, Upperman C, Zhu H, Gerber SA, Gygi S, Yuan J. A novel role for RIP1 kinase in mediating TNFalpha production. Cell Death Dis 2012; 3:e320; PMID:22695613; http://dx.doi.org/10.1038/cddis.2012.64
   PubMed Web of Science ®Google Scholar
• Christofferson DE, Yuan J. Necroptosis as an alternative form of programmed cell death. Curr Opin Cell Biol 2010; 22:263-8; PMID:20045303; http://dx.doi.org/10.1016/j.ceb.2009.12.003
   PubMed Web of Science ®Google Scholar
• Yang Y, Xia F, Hermance N, Mabb A, Simonson S, Morrissey S, Gandhi P, Munson M, Miyamoto S, Kelliher MA. A cytosolic ATM/NEMO/RIP1 complex recruits TAK1 to mediate the NF-kappaB and p38 mitogen-activated protein kinase (MAPK)/MAPK-activated protein 2 responses to DNA damage. Mol Cell Biol 2011; 31:2774-86; PMID:21606198; http://dx.doi.org/10.1128/MCB.01139-10
   PubMed Web of Science ®Google Scholar
• Niu J, Shi Y, Iwai K, Wu ZH. LUBAC regulates NF-kappaB activation upon genotoxic stress by promoting linear ubiquitination of NEMO. EMBO J 2011; 30:3741-53; PMID:21811235; http://dx.doi.org/10.1038/emboj.2011.264
   PubMed Web of Science ®Google Scholar
• Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J, Gillard JW, Jaquith JB, Morris SJ, Barker PA. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell 2008; 30:689-700; PMID:18570872; http://dx.doi.org/10.1016/j.molcel.2008.05.014
   PubMed Web of Science ®Google Scholar
• Harding HP, Calfon M, Urano F, Novoa I, Ron D. Transcriptional and translational control in the Mammalian unfolded protein response. Annu Rev Cell Dev Biol 2002; 18:575-99; PMID:12142265; http://dx.doi.org/10.1146/annurev.cellbio.18.011402.160624
   PubMed Web of Science ®Google Scholar
• Croft A, Tay KH, Boyd SC, Guo ST, Jiang CC, Lai F, Tseng HY, Jin L, Rizos H, Hersey P, et al. Oncogenic activation of MEK/ERK primes melanoma cells for adaptation to endoplasmic reticulum stress. J Invest Dermatol 2014; 134:488-97; PMID:23921951; http://dx.doi.org/10.1038/jid.2013.325
   PubMed Web of Science ®Google Scholar
• Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011; 334:1081-6; PMID:22116877; http://dx.doi.org/10.1126/science.1209038
   PubMed Web of Science ®Google Scholar
• Wang S, Kaufman RJ. The impact of the unfolded protein response on human disease. J Cell Biol 2012; 197:857-67; PMID:22733998; http://dx.doi.org/10.1083/jcb.201110131
   PubMed Web of Science ®Google Scholar
• Boyce M, Yuan J. Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death Differ 2006; 13:363-73; PMID:16397583; http://dx.doi.org/10.1038/sj.cdd.4401817
   PubMed Web of Science ®Google Scholar
• Hitomi J, Katayama T, Eguchi Y, Kudo T, Taniguchi M, Koyama Y, Manabe T, Yamagishi S, Bando Y, Imaizumi K, et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 2004; 165:347-56; PMID:15123740; http://dx.doi.org/10.1083/jcb.200310015
   PubMed Web of Science ®Google Scholar
• Tay KH, Luan Q, Croft A, Jiang CC, Jin L, Zhang XD, Tseng HY. Sustained IRE1 and ATF6 signaling is important for survival of melanoma cells undergoing ER stress. Cell Signal 2014; 26:287-94; PMID:24240056; http://dx.doi.org/10.1016/j.cellsig.2013.11.008
   PubMed Web of Science ®Google Scholar
• Li B, Pi Z, Liu L, Zhang B, Huang X, Hu P, Chevet E, Yi P, Liu J. FGF-2 prevents cancer cells from ER stress-mediated apoptosis via enhancing proteasome-mediated Nck degradation. Biochem J 2013; 452:139-45; PMID:23448571; http://dx.doi.org/10.1042/BJ20120680
   PubMed Web of Science ®Google Scholar
• Jiang CC, Chen LH, Gillespie S, Wang YF, Kiejda KA, Zhang XD, Hersey P. Inhibition of MEK sensitizes human melanoma cells to endoplasmic reticulum stress-induced apoptosis. Cancer Res 2007; 67:9750-61; PMID:17942905; http://dx.doi.org/10.1158/0008-5472.CAN-07-2047
   PubMed Web of Science ®Google Scholar
• Jiang CC, Lucas K, Avery-Kiejda KA, Wade M, deBock CE, Thorne RF, Allen J, Hersey P, Zhang XD. Up-regulation of Mcl-1 is critical for survival of human melanoma cells upon endoplasmic reticulum stress. Cancer Res 2008; 68:6708-17; PMID:18701495; http://dx.doi.org/10.1158/0008-5472.CAN-08-0349
   PubMed Web of Science ®Google Scholar
• Jiang CC, Yang F, Thorne RF, Zhu BK, Hersey P, Zhang XD. Human melanoma cells under endoplasmic reticulum stress acquire resistance to microtubule-targeting drugs through XBP-1-mediated activation of Akt. Neoplasia 2009; 11:436-47; PMID:19412428; http://dx.doi.org/10.1593/neo.09208
   PubMed Web of Science ®Google Scholar
• Dong L, Jiang CC, Thorne RF, Croft A, Yang F, Liu H, de Bock CE, Hersey P, Zhang XD. Ets-1 mediates upregulation of Mcl-1 downstream of XBP-1 in human melanoma cells upon ER stress. Oncogene 2011; 30:3716-26; PMID:21423203; http://dx.doi.org/10.1038/onc.2011.87
   PubMed Web of Science ®Google Scholar
• Ogata M, Hino S, Saito A, Morikawa K, Kondo S, Kanemoto S, Murakami T, Taniguchi M, Tanii I, Yoshinaga K, et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 2006; 26:9220-31; PMID:17030611; http://dx.doi.org/10.1128/MCB.01453-06
   PubMed Web of Science ®Google Scholar
• Kouroku Y, Fujita E, Tanida I, Ueno T, Isoai A, Kumagai H, Ogawa S, Kaufman RJ, Kominami E, Momoi T. ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ 2007; 14:230-9; PMID:16794605; http://dx.doi.org/10.1038/sj.cdd.4401984
   PubMed Web of Science ®Google Scholar
• Rabinowitz JD, White E. Autophagy and metabolism. Science 2010; 330:1344-8; PMID:21127245; http://dx.doi.org/10.1126/science.1193497
   PubMed Web of Science ®Google Scholar
• Klionsky DJ, Abdalla FC, Abeliovich H, Abraham RT, Acevedo-Arozena A, Adeli K, Agholme L, Agnello M, Agostinis P, Aguirre-Ghiso JA, et al. Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy 2012; 8:445-544; PMID:22966490; http://dx.doi.org/10.4161/auto.19496
   PubMed Web of Science ®Google Scholar
• Kroemer G, Jaattela M. Lysosomes and autophagy in cell death control. Nat Rev Cancer 2005; 5:886-97; PMID:16239905; http://dx.doi.org/10.1038/nrc1738
   PubMed Web of Science ®Google Scholar
• Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008; 132:27-42; PMID:18191218; http://dx.doi.org/10.1016/j.cell.2007.12.018
   PubMed Web of Science ®Google Scholar
• Rikiishi H. Novel Insights into the Interplay between Apoptosis and Autophagy. Int J Cell Biol 2012; 2012:317645; PMID:22496691; http://dx.doi.org/10.1155/2012/317645
   PubMedGoogle Scholar
• Jin S, White E. Tumor suppression by autophagy through the management of metabolic stress. Autophagy 2008; 4:563-6; PMID:18326941; http://dx.doi.org/10.4161/auto.5830
   PubMed Web of Science ®Google Scholar
• Kondo Y, Kanzawa T, Sawaya R, Kondo S. The role of autophagy in cancer development and response to therapy. Nat Rev Cancer 2005; 5:726-34; PMID:16148885; http://dx.doi.org/10.1038/nrc1692
   PubMed Web of Science ®Google Scholar
• Dikic I, Johansen T, Kirkin V. Selective autophagy in cancer development and therapy. Cancer Res 2010; 70:3431-4; PMID:20424122; http://dx.doi.org/10.1158/0008-5472.CAN-09-4027
   PubMed Web of Science ®Google Scholar
• Hart LS, Cunningham JT, Datta T, Dey S, Tameire F, Lehman SL, Qiu B, Zhang H, Cerniglia G, Bi M, et al. ER stress-mediated autophagy promotes Myc-dependent transformation and tumor growth. J Clin Invest 2012; 122:4621-34; PMID:23143306; http://dx.doi.org/10.1172/JCI62973
   PubMed Web of Science ®Google Scholar
• Verfaillie T, Salazar M, Velasco G, Agostinis P. Linking ER Stress to Autophagy: Potential Implications for Cancer Therapy. Int J Cell Biol 2010; 2010:930509; PMID:20145727; http://dx.doi.org/10.1155/2010/930509
   PubMedGoogle Scholar
• Li J, Ni M, Lee B, Barron E, Hinton DR, Lee AS. The unfolded protein response regulator GRP78/BiP is required for endoplasmic reticulum integrity and stress-induced autophagy in mammalian cells. Cell Death Differ 2008; 15:1460-71; PMID:18551133; http://dx.doi.org/10.1038/cdd.2008.81
   PubMed Web of Science ®Google Scholar
• Muscarella DE, Bloom SE. The contribution of c-Jun N-terminal kinase activation and subsequent Bcl-2 phosphorylation to apoptosis induction in human B-cells is dependent on the mode of action of specific stresses. Toxicol Appl Pharmacol 2008; 228:93-104; PMID:18201741; http://dx.doi.org/10.1016/j.taap.2007.11.032
   PubMed Web of Science ®Google Scholar
• Yamamoto K, Ichijo H, Korsmeyer SJ. BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol 1999; 19:8469-78; PMID:10567572
   PubMed Web of Science ®Google Scholar
• Luo S, Garcia-Arencibia M, Zhao R, Puri C, Toh PP, Sadiq O, Rubinsztein DC. Bim inhibits autophagy by recruiting Beclin 1 to microtubules. Mol Cell 2012; 47:359-70; PMID:22742832; http://dx.doi.org/10.1016/j.molcel.2012.05.040
   PubMed Web of Science ®Google Scholar
• Zalckvar E, Berissi H, Mizrachy L, Idelchuk Y, Koren I, Eisenstein M, Sabanay H, Pinkas-Kramarski R, Kimchi A. DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. EMBO Rep 2009; 10:285-92; PMID:19180116; http://dx.doi.org/10.1038/embor.2008.246
   PubMed Web of Science ®Google Scholar
• Pattingre S, Tassa A, Qu X, Garuti R, Liang XH, Mizushima N, Packer M, Schneider MD, Levine B. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 2005; 122:927-39; PMID:16179260; http://dx.doi.org/10.1016/j.cell.2005.07.002
   PubMed Web of Science ®Google Scholar
• Tai WT, Shiau CW, Chen HL, Liu CY, Lin CS, Cheng AL, Chen PJ, Chen KF. Mcl-1-dependent activation of Beclin 1 mediates autophagic cell death induced by sorafenib and SC-59 in hepatocellular carcinoma cells. Cell Death Dis 2013; 4:e485; PMID:23392173; http://dx.doi.org/10.1038/cddis.2013.18
   PubMed Web of Science ®Google Scholar
• Vihervaara A, Sistonen L. HSF1 at a glance. J Cell Sci 2014; 127:261-6; PMID:24421309; http://dx.doi.org/10.1242/jcs.132605
   PubMed Web of Science ®Google Scholar
• Mendillo ML, Santagata S, Koeva M, Bell GW, Hu R, Tamimi RM, Fraenkel E, Ince TA, Whitesell L, Lindquist S. HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers. Cell 2012; 150:549-62; PMID:22863008; http://dx.doi.org/10.1016/j.cell.2012.06.031
   PubMed Web of Science ®Google Scholar
• Pelham HR. A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene. Cell 1982; 30:517-28; PMID:6814763; http://dx.doi.org/10.1016/0092-8674(82)90249-5
   PubMed Web of Science ®Google Scholar
• Guettouche T, Boellmann F, Lane WS, Voellmy R. Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress. BMC Biochem 2005; 6:4; PMID:15760475; http://dx.doi.org/10.1186/1471-2091-6-4
   PubMedGoogle Scholar
• Jiang CC, Mao ZG, Avery-Kiejda KA, Wade M, Hersey P, Zhang XD. Glucose-regulated protein 78 antagonizes cisplatin and adriamycin in human melanoma cells. Carcinogenesis 2009; 30:197-204; PMID:18842681; http://dx.doi.org/10.1093/carcin/bgn220
   PubMed Web of Science ®Google Scholar
• Wang Z, Jiang H, Chen S, Du F, Wang X. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 2012; 148:228-43; PMID:22265414; http://dx.doi.org/10.1016/j.cell.2011.11.030
   PubMed Web of Science ®Google Scholar
• Gozuacik D, Bialik S, Raveh T, Mitou G, Shohat G, Sabanay H, Mizushima N, Yoshimori T, Kimchi A. DAP-kinase is a mediator of endoplasmic reticulum stress-induced caspase activation and autophagic cell death. Cell Death Differ 2008; 15:1875-86; PMID:18806755; http://dx.doi.org/10.1038/cdd.2008.121
   PubMed Web of Science ®Google Scholar
• Ding WX, Ni HM, Gao W, Hou YF, Melan MA, Chen X, Stolz DB, Shao ZM, Yin XM. Differential effects of endoplasmic reticulum stress-induced autophagy on cell survival. J Biol Chem 2007; 282:4702-10; PMID:17135238; http://dx.doi.org/10.1074/jbc.M609267200
   PubMed Web of Science ®Google Scholar
• Bicknell AA, Tourtellotte J, Niwa M. Late phase of the endoplasmic reticulum stress response pathway is regulated by Hog1 MAP kinase. J Biol Chem 2010; 285:17545-55; PMID:20382742; http://dx.doi.org/10.1074/jbc.M109.084681
   PubMed Web of Science ®Google Scholar
• Wei Y, Sinha S, Levine B. Dual role of JNK1-mediated phosphorylation of Bcl-2 in autophagy and apoptosis regulation. Autophagy 2008; 4:949-51; PMID:18769111; http://dx.doi.org/10.4161/auto.6788
   PubMed Web of Science ®Google Scholar
• Yang Q, Kim YS, Lin Y, Lewis J, Neckers L, Liu ZG. Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. EMBO Rep 2006; 7:622-7; PMID:16680093
   PubMed Web of Science ®Google Scholar
• He W, Wang Q, Srinivasan B, Xu J, Padilla MT, Li Z, Wang X, Liu Y, Gou X, Shen HM, et al. A JNK-mediated autophagy pathway that triggers c-IAP degradation and necroptosis for anticancer chemotherapy. Oncogene 2014; 33:3004-13; PMID:23831571; http://dx.doi.org/10.1038/onc.2013.256
   PubMed Web of Science ®Google Scholar
• Tenev T, Bianchi K, Darding M, Broemer M, Langlais C, Wallberg F, Zachariou A, Lopez J, MacFarlane M, Cain K, et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol Cell 2011; 43:432-48; PMID:21737329; http://dx.doi.org/10.1016/j.molcel.2011.06.006
   PubMed Web of Science ®Google Scholar
• Degterev A, Hitomi J, Germscheid M, Ch'en IL, Korkina O, Teng X, Abbott D, Cuny GD, Yuan C, Wagner G, et al. Identification of RIP1 kinase as a specific cellular target of necrostatins. Nat Chem Biol 2008; 4:313-21; PMID:18408713; http://dx.doi.org/10.1038/nchembio.83
   PubMed Web of Science ®Google Scholar
• Huang H, Kang R, Wang J, Luo G, Yang W, Zhao Z. Hepatitis C virus inhibits AKT-tuberous sclerosis complex (TSC), the mechanistic target of rapamycin (MTOR) pathway, through endoplasmic reticulum stress to induce autophagy. Autophagy 2013; 9:175-95; PMID:23169238; http://dx.doi.org/10.4161/auto.22791
   PubMed Web of Science ®Google Scholar
• Hoyer-Hansen M, Bastholm L, Szyniarowski P, Campanella M, Szabadkai G, Farkas T, Bianchi K, Fehrenbacher N, Elling F, Rizzuto R, et al. Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2. Mol Cell 2007; 25:193-205; PMID:17244528; http://dx.doi.org/10.1016/j.molcel.2006.12.009
   PubMed Web of Science ®Google Scholar
• Schroder M, Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 2005; 74:739-89; PMID:15952902; http://dx.doi.org/10.1146/annurev.biochem.73.011303.074134
   PubMed Web of Science ®Google Scholar
• Dai B, Gong A, Jing Z, Aldape KD, Kang SH, Sawaya R, Huang S. Forkhead box M1 is regulated by heat shock factor 1 and promotes glioma cells survival under heat shock stress. J Biol Chem 2013; 288:1634-42; PMID:23192351; http://dx.doi.org/10.1074/jbc.M112.379362
   PubMed Web of Science ®Google Scholar
• Xiao X, Zuo X, Davis AA, McMillan DR, Curry BB, Richardson JA, Benjamin IJ. HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. EMBO J 1999; 18:5943-52; PMID:10545106; http://dx.doi.org/10.1093/emboj/18.21.5943
   PubMed Web of Science ®Google Scholar
• Dai C, Santagata S, Tang Z, Shi J, Cao J, Kwon H, Bronson RT, Whitesell L, Lindquist S. Loss of tumor suppressor NF1 activates HSF1 to promote carcinogenesis. J Clin Invest 2012; 122:3742-54; PMID:22945628; http://dx.doi.org/10.1172/JCI62727
   PubMed Web of Science ®Google Scholar
• Biton S, Ashkenazi A. NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-alpha feedforward signaling. Cell 2011; 145:92-103; PMID:21458669; http://dx.doi.org/10.1016/j.cell.2011.02.023
   PubMed Web of Science ®Google Scholar
• Park S, Hatanpaa KJ, Xie Y, Mickey BE, Madden CJ, Raisanen JM, Ramnarain DB, Xiao G, Saha D, Boothman DA, et al. The receptor interacting protein 1 inhibits p53 induction through NF-kappaB activation and confers a worse prognosis in glioblastoma. Cancer Res 2009; 69:2809-16; PMID:19339267; http://dx.doi.org/10.1158/0008-5472.CAN-08-4079
   PubMed Web of Science ®Google Scholar
• Hersey P, Zhang XD. Adaptation to ER stress as a driver of malignancy and resistance to therapy in human melanoma. Pigment Cell Melanoma Res 2008; 21:358-67; PMID:18476909; http://dx.doi.org/10.1111/j.1755-148X.2008.00467.x
   PubMed Web of Science ®Google Scholar
• Kelliher MA, Grimm S, Ishida Y, Kuo F, Stanger BZ, Leder P. The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity 1998; 8:297-303; PMID:9529147; http://dx.doi.org/10.1016/S1074-7613(00)80535-X
   PubMed Web of Science ®Google Scholar
• Nozaki S, Sledge Jr GW, Nakshatri H. Repression of GADD153/CHOP by NF-kappaB: a possible cellular defense against endoplasmic reticulum stress-induced cell death. Oncogene 2001; 20:2178-85; PMID:11360202; http://dx.doi.org/10.1038/sj.onc.1204292
   PubMed Web of Science ®Google Scholar
• Maiuri MC, Le Toumelin G, Criollo A, Rain JC, Gautier F, Juin P, Tasdemir E, Pierron G, Troulinaki K, Tavernarakis N, et al. Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1. EMBO J 2007; 26:2527-39; PMID:17446862; http://dx.doi.org/10.1038/sj.emboj.7601689
   PubMed Web of Science ®Google Scholar
• Oberstein A, Jeffrey PD, Shi Y. Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. J Biol Chem 2007; 282:13123-32; PMID:17337444; http://dx.doi.org/10.1074/jbc.M700492200
   PubMed Web of Science ®Google Scholar
• Zong WX, Lindsten T, Ross AJ, MacGregor GR, Thompson CB. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev 2001; 15:1481-6; PMID:11410528; http://dx.doi.org/10.1101/gad.897601
   PubMed Web of Science ®Google Scholar
• Merino D, Giam M, Hughes PD, Siggs OM, Heger K, O'Reilly LA, Adams JM, Strasser A, Lee EF, Fairlie WD, et al. The role of BH3-only protein Bim extends beyond inhibiting Bcl-2-like prosurvival proteins. J Cell Biol 2009; 186:355-62; PMID:19651893; http://dx.doi.org/10.1083/jcb.200905153
   PubMed Web of Science ®Google Scholar
• Hubner A, Barrett T, Flavell RA, Davis RJ. Multisite phosphorylation regulates Bim stability and apoptotic activity. Mol Cell 2008; 30:415-25; PMID:18498746; http://dx.doi.org/10.1016/j.molcel.2008.03.025
   PubMed Web of Science ®Google Scholar
• Ley R, Balmanno K, Hadfield K, Weston C, Cook SJ. Activation of the ERK1/2 signaling pathway promotes phosphorylation and proteasome-dependent degradation of the BH3-only protein, Bim. J Biol Chem 2003; 278:18811-6; PMID:12646560; http://dx.doi.org/10.1074/jbc.M301010200
   PubMed Web of Science ®Google Scholar
• Tay KH, Jin L, Tseng HY, Jiang CC, Ye Y, Thorne RF, Liu T, Guo ST, Verrills NM, Hersey P, et al. Suppression of PP2A is critical for protection of melanoma cells upon endoplasmic reticulum stress. Cell Death Dis 2012; 3:e337; PMID:22739989; http://dx.doi.org/10.1038/cddis.2012.79
   PubMedGoogle Scholar
• Cagnol S, Chambard JC. ERK and cell death: mechanisms of ERK-induced cell death–apoptosis, autophagy and senescence. FEBS J 2010; 277:2-21; PMID:19843174; http://dx.doi.org/10.1111/j.1742-4658.2009.07366.x
   PubMed Web of Science ®Google Scholar
• Ellington AA, Berhow MA, Singletary KW. Inhibition of Akt signaling and enhanced ERK1/2 activity are involved in induction of macroautophagy by triterpenoid B-group soyasaponins in colon cancer cells. Carcinogenesis 2006; 27:298-306; PMID:16113053; http://dx.doi.org/10.1093/carcin/bgi214
   PubMed Web of Science ®Google Scholar
• Sivaprasad U, Basu A. Inhibition of ERK attenuates autophagy and potentiates tumour necrosis factor-alpha-induced cell death in MCF-7 cells. J Cell Mol Med 2008; 12:1265-71; PMID:18266953; http://dx.doi.org/10.1111/j.1582-4934.2008.00282.x
   PubMed Web of Science ®Google Scholar
• Kim DS, Kim JH, Lee GH, Kim HT, Lim JM, Chae SW, Chae HJ, Kim HR. p38 Mitogen-activated protein kinase is involved in endoplasmic reticulum stress-induced cell death and autophagy in human gingival fibroblasts. Biol Pharm Bull 2010; 33:545-9; PMID:20410583; http://dx.doi.org/10.1248/bpb.33.545
   PubMed Web of Science ®Google Scholar
• Zhong W, Zhu H, Sheng F, Tian Y, Zhou J, Chen Y, Li S, Lin J. Activation of the MAPK11/12/13/14 (p38 MAPK) pathway regulates the transcription of autophagy genes in response to oxidative stress induced by a novel copper complex in HeLa cells. Autophagy 2014; 10:1285-300; PMID:24905917; http://dx.doi.org/10.4161/auto.28789
   PubMed Web of Science ®Google Scholar
• Tabas I, Ron D. Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat Cell Biol 2011; 13:184-90; PMID:21364565; http://dx.doi.org/10.1038/ncb0311-184
   PubMed Web of Science ®Google Scholar
• Lamb JA, Ventura JJ, Hess P, Flavell RA, Davis RJ. JunD mediates survival signaling by the JNK signal transduction pathway. Mol Cell 2003; 11:1479-89; PMID:12820962; http://dx.doi.org/10.1016/S1097-2765(03)00203-X
   PubMed Web of Science ®Google Scholar
• Yu C, Minemoto Y, Zhang J, Liu J, Tang F, Bui TN, Xiang J, Lin A. JNK suppresses apoptosis via phosphorylation of the proapoptotic Bcl-2 family protein BAD. Mol Cell 2004; 13:329-40; PMID:14967141; http://dx.doi.org/10.1016/S1097-2765(04)00028-0
   PubMed Web of Science ®Google Scholar
• Engerud H, Tangen IL, Berg A, Kusonmano K, Halle MK, Oyan AM, Kalland KH, Stefansson I, Trovik J, Salvesen HB, et al. High level of HSF1 associates with aggressive endometrial carcinoma and suggests potential for HSP90 inhibitors. Br J Cancer 2014; 111:78-84; PMID:24853175; http://dx.doi.org/10.1038/bjc.2014.262
   PubMed Web of Science ®Google Scholar
• Santagata S, Hu R, Lin NU, Mendillo ML, Collins LC, Hankinson SE, Schnitt SJ, Whitesell L, Tamimi RM, Lindquist S, et al. High levels of nuclear heat-shock factor 1 (HSF1) are associated with poor prognosis in breast cancer. Proc Natl Acad Sci U S A 2011; 108:18378-83; PMID:22042860; http://dx.doi.org/10.1073/pnas.1115031108
   PubMed Web of Science ®Google Scholar
• Jiang CC, Chen LH, Gillespie S, Kiejda KA, Mhaidat N, Wang YF, Thorne R, Zhang XD, Hersey P. Tunicamycin sensitizes human melanoma cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by up-regulation of TRAIL-R2 via the unfolded protein response. Cancer Res 2007; 67:5880-8; PMID:17575157; http://dx.doi.org/10.1158/0008-5472.CAN-07-0213
   PubMed Web of Science ®Google Scholar
• Liu CY, Kaufman RJ. The unfolded protein response. J Cell Sci 2003; 116:1861-2; PMID:12692187; http://dx.doi.org/10.1242/jcs.00408
   PubMed Web of Science ®Google Scholar
• Tseng HY, Jiang CC, Croft A, Tay KH, Thorne RF, Yang F, Liu H, Hersey P, Zhang XD. Contrasting effects of nutlin-3 on TRAIL- and docetaxel-induced apoptosis due to upregulation of TRAIL-R2 and Mcl-1 in human melanoma cells. Mol Cancer Ther 2010; 9:3363-74; PMID:21159614; http://dx.doi.org/10.1158/1535-7163.MCT-10-0646
   PubMed Web of Science ®Google Scholar
• Lai F, Guo ST, Jin L, Jiang CC, Wang CY, Croft A, Chi MN, Tseng HY, Farrelly M, Atmadibrata B, et al. Cotargeting histone deacetylases and oncogenic BRAF synergistically kills human melanoma cells by necrosis independently of RIPK1 and RIPK3. Cell Death Dis 2013; 4:e655; PMID:23744355; http://dx.doi.org/10.1038/cddis.2013.192
   PubMedGoogle Scholar
• Ye Y, Jin L, Wilmott JS, Hu WL, Yosufi B, Thorne RF, Liu T, Rizos H, Yan XG, Dong L, et al. PI(4,5)P2 5-phosphatase A regulates PI3K/Akt signalling and has a tumour suppressive role in human melanoma. Nat Commun 2013; 4:1508; PMID:23443536; http://dx.doi.org/10.1038/ncomms2489
   PubMed Web of Science ®Google Scholar
• Yang F, Tay KH, Dong L, Thorne RF, Jiang CC, Yang E, Tseng HY, Liu H, Christopherson R, Hersey P, et al. Cystatin B inhibition of TRAIL-induced apoptosis is associated with the protection of FLIP(L) from degradation by the E3 ligase itch in human melanoma cells. Cell Death Differ 2010; 17:1354-67; PMID:20300110; http://dx.doi.org/10.1038/cdd.2010.29
   PubMed Web of Science ®Google Scholar