참고문헌
- Anderson P, Kedersha N. Stress granules: the Tao of RNA triage. Trends Biochem Sci. 2008. 33: 141-150. https://doi.org/10.1016/j.tibs.2007.12.003
- Anderson P, Kedersha N. Stress granules. Curr Biol. 2009. 19: R397-398. https://doi.org/10.1016/j.cub.2009.03.013
- Arimoto K, Fukuda H, Imajoh-Ohmi S, Saito H,Takekawa M. Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat Cell Biol. 2008. 10: 1324-1332. https://doi.org/10.1038/ncb1791
- Buchan JR, Kolaitis RM, Taylor JP, Parker R. Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function. Cell. 2013. 153: 1461-1474. https://doi.org/10.1016/j.cell.2013.05.037
- Buchan JR, Parker R. Eukaryotic stress granules: the ins and outs of translation. Mol Cell. 2009. 36: 932-941. https://doi.org/10.1016/j.molcel.2009.11.020
- Calkhoven CF, Muller C, Leutz A. Translational control of gene expression and disease. Trends Mol Med. 2002. 8: 577-583. https://doi.org/10.1016/S1471-4914(02)02424-3
- de Nadal E, Ammerer G, Posas F. Controlling gene expression in response to stress. Nat Rev Genet. 2011. 12: 833-845.
- Dolzhanskaya N, Merz G, Aletta JM, Denman RB. Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP. J Cell Sci. 2006. 119: 1933-1946. https://doi.org/10.1242/jcs.02882
- Emara MM, Fujimura K, Sciaranghella D, Ivanova V, Ivanov P, Anderson P. Hydrogen peroxide induces stress granule formation independent of eIF2alpha phosphorylation. Biochem Biophys Res Commun. 2012. 423: 763-769. https://doi.org/10.1016/j.bbrc.2012.06.033
- Fujimura K, Sasaki AT, Anderson P. Selenite targets eIF4E-binding protein-1 to inhibit translation initiation and induce the assembly of non-canonical stress granules. Nucleic Acids Res. 2012. 40: 8099-8110. https://doi.org/10.1093/nar/gks566
- Gilks N, Kedersha N, Ayodele M, Shen L, Stoecklin G, Dember LM, Anderson P. Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol Biol Cell. 2004. 15: 5383-5398. https://doi.org/10.1091/mbc.E04-08-0715
- Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M, Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell. 2000a. 6: 1099-1108. https://doi.org/10.1016/S1097-2765(00)00108-8
- Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell. 2000b. 5: 897-904. https://doi.org/10.1016/S1097-2765(00)80330-5
- Hilliker A, Parker R. Stressed out? Make some modifications! Nat Cell Biol. 2008. 10: 1129-1130. https://doi.org/10.1038/ncb1008-1129
- Hofmann S, Cherkasova V, Bankhead P, Bukau B, Stoecklin G. Translation suppression promotes stress granule formation and cell survival in response to cold shock. Mol Biol Cell. 2012. 23: 3786-3800. https://doi.org/10.1091/mbc.E12-04-0296
- Holcik M, Sonenberg N. Translational control in stress and apoptosis. Nat Rev Mol Cell Biol. 2005. 6: 318-327. https://doi.org/10.1038/nrm1618
- Jackson RJ, Hellen CU, Pestova TV. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol. 2010. 11: 113-127. https://doi.org/10.1038/nrm2838
- Kedersha N, Anderson P. Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem Soc Trans. 2002. 30: 963-969. https://doi.org/10.1042/bst0300963
- Kedersha N, Anderson P. Mammalian stress granules and processing bodies. Methods Enzymol. 2007. 431: 61-81. https://doi.org/10.1016/S0076-6879(07)31005-7
- Kedersha N, Cho MR, Li W, Yacono PW, Chen S, Gilks N, Golan DE, Anderson P. Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules. J Cell Biol. 2000. 151: 1257-1268. https://doi.org/10.1083/jcb.151.6.1257
- Kedersha N, Ivanov P, Anderson P. Stress granules and cell signaling: more than just a passing phase? Trends Biochem Sci. 2013. 38: 494-506. https://doi.org/10.1016/j.tibs.2013.07.004
- Kedersha N, Stoecklin G, Ayodele M, Yacono P, Lykke-Andersen J, Fritzler MJ, Scheuner D, Kaufman RJ, Golan DE, Anderson P. Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J Cell Biol. 2005. 169: 871-884. https://doi.org/10.1083/jcb.200502088
- Kedersha NL, Gupta M, Li W, Miller I, Anderson P. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J Cell Biol. 1999. 147: 1431-1442. https://doi.org/10.1083/jcb.147.7.1431
- Kim WJ, Back SH, Kim V, Ryu I, Jang SK. Sequestration of TRAF2 into stress granules interrupts tumor necrosis factor signaling under stress conditions. Mol Cell Biol. 2005. 25: 2450-2462. https://doi.org/10.1128/MCB.25.6.2450-2462.2005
- Kwon S, Zhang Y, Matthias P. The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. Genes Dev. 2007. 21: 3381-3394. https://doi.org/10.1101/gad.461107
- Li CH, Ohn T, Ivanov P, Tisdale S, Anderson P. eIF5A promotes translation elongation, polysome disassembly and stress granule assembly. PloS One. 2010. 5: e9942. https://doi.org/10.1371/journal.pone.0009942
- McEwen E, Kedersha N, Song B, Scheuner D, Gilks N, Han A, Chen JJ, Anderson P, Kaufman RJ. Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J Biol Chem. 2005. 280: 16925-16933. https://doi.org/10.1074/jbc.M412882200
- Mollet S, Cougot N, Wilczynska A, Dautry F, Kress M, Bertrand E, Weil D. Translationally repressed mRNA transiently cycles through stress granules during stress. Mol Biol Cell. 2008. 19: 4469-4479. https://doi.org/10.1091/mbc.E08-05-0499
- Ohn T, Anderson P. The role of posttranslational modifications in the assembly of stress granules. Wiley Interdiscip Rev RNA. 2010. 1: 486-493. https://doi.org/10.1002/wrna.23
- Ohn T, Kedersha N, Hickman T, Tisdale S, Anderson P. A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat Cell Biol. 2008. 10: 1224-1231. https://doi.org/10.1038/ncb1783
- Parker F, Maurier F, Delumeau I, Duchesne M, Faucher D, Debussche L, Dugue A, Schweighoffer F, Tocque B. A Ras- GTPase-activating protein SH3-domain-binding protein. Mol Cell Biol. 1996. 16: 2561-2569. https://doi.org/10.1128/MCB.16.6.2561
- Ramaswami M, Taylor JP,Parker R. Altered ribostasis: RNAprotein granules in degenerative disorders. Cell. 2013. 154: 727-736. https://doi.org/10.1016/j.cell.2013.07.038
- Reineke LC, Dougherty JD, Pierre P, Lloyd RE. Large G3BPinduced granules trigger eIF2alpha phosphorylation. Mol Biol Cell. 2012. 23: 3499-3510. https://doi.org/10.1091/mbc.E12-05-0385
- Richter JD, Sonenberg N. Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature. 2005. 433: 477-480. https://doi.org/10.1038/nature03205
- Riedl SJ, Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat Rev Mol Cell Biol. 2004. 5: 897-907. https://doi.org/10.1038/nrm1496
- Sonenberg N, Hinnebusch AG. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell. 2009. 136: 731-745. https://doi.org/10.1016/j.cell.2009.01.042
- Spriggs KA, Bushell M, Willis AE. Translational regulation of gene expression during conditions of cell stress. Mol Cell. 2010. 40: 228-237. https://doi.org/10.1016/j.molcel.2010.09.028
- Srivastava SP, Kumar KU, Kaufman RJ. Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNAdependent protein kinase. J Biol Chem. 1998. 273: 2416-2423. https://doi.org/10.1074/jbc.273.4.2416
- Stoecklin G, Kedersha N. Relationship of GW/P-bodies with stress granules. Adv Exp Med Biol. 2013. 768: 197-211. https://doi.org/10.1007/978-1-4614-5107-5_12
- Stoecklin G, Stubbs T, Kedersha N, Wax S, Rigby WF, Blackwell TK, Anderson P. MK2-induced tristetraprolin: 14-3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J. 2004. 23: 1313-1324. https://doi.org/10.1038/sj.emboj.7600163
- Tourriere H, Chebli K, Zekri L, Courselaud B, Blanchard JM, Bertrand E, Tazi J. The RasGAP-associated endoribonuclease G3BP assembles stress granules. J Cell Biol. 2003. 160: 823-831. https://doi.org/10.1083/jcb.200212128
- Wek RC, Jiang HY,Anthony TG. Coping with stress: eIF2 kinases and translational control. Biochem Soc Trans. 2006. 34: 7-11. https://doi.org/10.1042/BST0340007
- Wippich F, Bodenmiller B, Trajkovska MG, Wanka S, Aebersold R, Pelkmans L. Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling. Cell. 2013. 152: 791-805. https://doi.org/10.1016/j.cell.2013.01.033