Heat-shock stress activates a novel nuclear import pathway mediated by Hikeshi

References

• Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S. Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep 2000; 1:287 - 92; http://dx.doi.org/10.1093/embo-reports/kvd058; PMID: 11256614
   PubMed Web of Science ®Google Scholar
• Hoelz A, Debler EW, Blobel G. The structure of the nuclear pore complex. Annu Rev Biochem 2011; 80:613 - 43; http://dx.doi.org/10.1146/annurev-biochem-060109-151030; PMID: 21495847
   PubMed Web of Science ®Google Scholar
• Wente SR, Rout MP. The nuclear pore complex and nuclear transport. Cold Spring Harb Perspect Biol 2010; 2:a000562; http://dx.doi.org/10.1101/cshperspect.a000562; PMID: 20630994
   PubMed Web of Science ®Google Scholar
• Imamoto N, Funakoshi T. Nuclear pore dynamics during the cell cycle. Curr Opin Cell Biol 2012; 24:453 - 9; http://dx.doi.org/10.1016/j.ceb.2012.06.004; PMID: 22770730
   PubMed Web of Science ®Google Scholar
• Ribbeck K, Görlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J 2002; 21:2664 - 71; http://dx.doi.org/10.1093/emboj/21.11.2664; PMID: 12032079
   PubMed Web of Science ®Google Scholar
• Chi NC, Adam EJ, Adam SA. Sequence and characterization of cytoplasmic nuclear protein import factor p97. J Cell Biol 1995; 130:265 - 74; http://dx.doi.org/10.1083/jcb.130.2.265; PMID: 7615630
   PubMed Web of Science ®Google Scholar
• Imamoto N, Shimamoto T, Kose S, Takao T, Tachibana T, Matsubae M, et al. The nuclear pore-targeting complex binds to nuclear pores after association with a karyophile. FEBS Lett 1995; 368:415 - 9; http://dx.doi.org/10.1016/0014-5793(95)00699-A; PMID: 7635189
   PubMed Web of Science ®Google Scholar
• Görlich D, Kostka S, Kraft R, Dingwall C, Laskey RA, Hartmann E, et al. Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr Biol 1995; 5:383 - 92; http://dx.doi.org/10.1016/S0960-9822(95)00079-0; PMID: 7627554
   PubMed Web of Science ®Google Scholar
• Görlich D, Kutay U. Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol 1999; 15:607 - 60; PMID: 10611974
   PubMed Web of Science ®Google Scholar
• Weis K. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 2003; 112:441 - 51; http://dx.doi.org/10.1016/S0092-8674(03)00082-5; PMID: 12600309
   PubMed Web of Science ®Google Scholar
• Stewart M. Molecular mechanism of the nuclear protein import cycle. Nat Rev Mol Cell Biol 2007; 8:195 - 208; http://dx.doi.org/10.1038/nrm2114; PMID: 17287812
   PubMed Web of Science ®Google Scholar
• Chook YM, Süel KE. Nuclear import by karyopherin-βs: recognition and inhibition. Biochim Biophys Acta 2011; 1813:1593 - 606; http://dx.doi.org/10.1016/j.bbamcr.2010.10.014; PMID: 21029754
   PubMed Web of Science ®Google Scholar
• Kose S, Furuta M, Imamoto N. Hikeshi, a nuclear import carrier for Hsp70s, protects cells from heat shock-induced nuclear damage. Cell 2012; 149:578 - 89; http://dx.doi.org/10.1016/j.cell.2012.02.058; PMID: 22541429
   PubMed Web of Science ®Google Scholar
• Richter K, Haslbeck M, Buchner J. The heat shock response: life on the verge of death. Mol Cell 2010; 40:253 - 66; http://dx.doi.org/10.1016/j.molcel.2010.10.006; PMID: 20965420
   PubMed Web of Science ®Google Scholar
• Akerfelt M, Morimoto RI, Sistonen L. Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 2010; 11:545 - 55; http://dx.doi.org/10.1038/nrm2938; PMID: 20628411
   PubMed Web of Science ®Google Scholar
• Morimoto RI. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 1998; 12:3788 - 96; http://dx.doi.org/10.1101/gad.12.24.3788; PMID: 9869631
   PubMed Web of Science ®Google Scholar
• Morimoto RI. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev 2008; 22:1427 - 38; http://dx.doi.org/10.1101/gad.1657108; PMID: 18519635
   PubMed Web of Science ®Google Scholar
• Lackner DH, Bähler J. Translational control of gene expression from transcripts to transcriptomes. Int Rev Cell Mol Biol 2008; 271:199 - 251; http://dx.doi.org/10.1016/S1937-6448(08)01205-7; PMID: 19081544
   PubMed Web of Science ®Google Scholar
• Mimnaugh EG, Chen HY, Davie JR, Celis JE, Neckers L. Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: effects on replication, transcription, translation, and the cellular stress response. Biochemistry 1997; 36:14418 - 29; http://dx.doi.org/10.1021/bi970998j; PMID: 9398160
   PubMed Web of Science ®Google Scholar
• Furuta M, Kose S, Koike M, Shimi T, Hiraoka Y, Yoneda Y, et al. Heat-shock induced nuclear retention and recycling inhibition of importin α. Genes Cells 2004; 9:429 - 41; http://dx.doi.org/10.1111/j.1356-9597.2004.00734.x; PMID: 15147272
   PubMed Web of Science ®Google Scholar
• Miyamoto Y, Saiwaki T, Yamashita J, Yasuda Y, Kotera I, Shibata S, et al. Cellular stresses induce the nuclear accumulation of importin α and cause a conventional nuclear import block. J Cell Biol 2004; 165:617 - 23; http://dx.doi.org/10.1083/jcb.200312008; PMID: 15184398
   PubMed Web of Science ®Google Scholar
• Czubryt MP, Austria JA, Pierce GN. Hydrogen peroxide inhibition of nuclear protein import is mediated by the mitogen-activated protein kinase, ERK2. J Cell Biol 2000; 148:7 - 16; http://dx.doi.org/10.1083/jcb.148.1.7; PMID: 10629214
   PubMed Web of Science ®Google Scholar
• Kelley JB, Paschal BM. Hyperosmotic stress signaling to the nucleus disrupts the Ran gradient and the production of RanGTP. Mol Biol Cell 2007; 18:4365 - 76; http://dx.doi.org/10.1091/mbc.E07-01-0089; PMID: 17761537
   PubMed Web of Science ®Google Scholar
• Kodiha M, Chu A, Matusiewicz N, Stochaj U. Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress. Cell Death Differ 2004; 11:862 - 74; http://dx.doi.org/10.1038/sj.cdd.4401432; PMID: 15088071
   PubMed Web of Science ®Google Scholar
• Lamian V, Small GM, Feldherr CM. Evidence for the existence of a novel mechanism for the nuclear import of Hsc70. Exp Cell Res 1996; 228:84 - 91; http://dx.doi.org/10.1006/excr.1996.0302; PMID: 8892974
   PubMed Web of Science ®Google Scholar
• Pelham HR. Hsp70 accelerates the recovery of nucleolar morphology after heat shock. EMBO J 1984; 3:3095 - 100; PMID: 6441707
   PubMed Web of Science ®Google Scholar
• Velazquez JM, Lindquist S. hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery. Cell 1984; 36:655 - 62; http://dx.doi.org/10.1016/0092-8674(84)90345-3; PMID: 6421488
   PubMed Web of Science ®Google Scholar
• Welch WJ, Feramisco JR. Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells. J Biol Chem 1984; 259:4501 - 13; PMID: 6368558
   PubMed Web of Science ®Google Scholar
• Adam SA, Marr RS, Gerace L. Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J Cell Biol 1990; 111:807 - 16; http://dx.doi.org/10.1083/jcb.111.3.807; PMID: 2391365
   PubMed Web of Science ®Google Scholar
• Kose S, Imamoto N, Tachibana T, Shimamoto T, Yoneda Y. Ran-unassisted nuclear migration of a 97-kD component of nuclear pore-targeting complex. J Cell Biol 1997; 139:841 - 9; http://dx.doi.org/10.1083/jcb.139.4.841; PMID: 9362503
   PubMed Web of Science ®Google Scholar
• Nakielny S, Dreyfuss G. Import and export of the nuclear protein import receptor transportin by a mechanism independent of GTP hydrolysis. Curr Biol 1998; 8:89 - 95; http://dx.doi.org/10.1016/S0960-9822(98)70039-9; PMID: 9427645
   PubMed Web of Science ®Google Scholar
• Nachury MV, Weis K. The direction of transport through the nuclear pore can be inverted. Proc Natl Acad Sci U S A 1999; 96:9622 - 7; http://dx.doi.org/10.1073/pnas.96.17.9622; PMID: 10449743
   PubMed Web of Science ®Google Scholar
• Kose S, Imamoto N, Tachibana T, Yoshida M, Yoneda Y. β-subunit of nuclear pore-targeting complex (importin-β) can be exported from the nucleus in a Ran-independent manner. J Biol Chem 1999; 274:3946 - 52; http://dx.doi.org/10.1074/jbc.274.7.3946; PMID: 9933584
   PubMed Web of Science ®Google Scholar
• Patel SS, Rexach MF. Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium. Mol Cell Proteomics 2008; 7:121 - 31; http://dx.doi.org/10.1074/mcp.M700407-MCP200; PMID: 17897934
   PubMed Web of Science ®Google Scholar
• Kampinga HH, Craig EA. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 2010; 11:579 - 92; http://dx.doi.org/10.1038/nrm2941; PMID: 20651708
   PubMed Web of Science ®Google Scholar
• Mayer MP. Gymnastics of molecular chaperones. Mol Cell 2010; 39:321 - 31; http://dx.doi.org/10.1016/j.molcel.2010.07.012; PMID: 20705236
   PubMed Web of Science ®Google Scholar
• Wilbanks SM, DeLuca-Flaherty C, McKay DB. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants. J Biol Chem 1994; 269:12893 - 8; PMID: 8175706
   PubMed Web of Science ®Google Scholar
• Cotto J, Fox S, Morimoto R. HSF1 granules: a novel stress-induced nuclear compartment of human cells. J Cell Sci 1997; 110:2925 - 34; PMID: 9359875
   PubMed Web of Science ®Google Scholar
• Shi Y, Mosser DD, Morimoto RI. Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev 1998; 12:654 - 66; http://dx.doi.org/10.1101/gad.12.5.654; PMID: 9499401
   PubMed Web of Science ®Google Scholar
• Mayer C, Bierhoff H, Grummt I. The nucleolus as a stress sensor: JNK2 inactivates the transcription factor TIF-IA and down-regulates rRNA synthesis. Genes Dev 2005; 19:933 - 41; http://dx.doi.org/10.1101/gad.333205; PMID: 15805466
   PubMed Web of Science ®Google Scholar
• Boulon S, Westman BJ, Hutten S, Boisvert FM, Lamond AI. The nucleolus under stress. Mol Cell 2010; 40:216 - 27; http://dx.doi.org/10.1016/j.molcel.2010.09.024; PMID: 20965417
   PubMed Web of Science ®Google Scholar
• Daniely Y, Borowiec JA. Formation of a complex between nucleolin and replication protein A after cell stress prevents initiation of DNA replication. J Cell Biol 2000; 149:799 - 810; http://dx.doi.org/10.1083/jcb.149.4.799; PMID: 10811822
   PubMed Web of Science ®Google Scholar
• Emmott E, Hiscox JA. Nucleolar targeting: the hub of the matter. EMBO Rep 2009; 10:231 - 8; http://dx.doi.org/10.1038/embor.2009.14; PMID: 19229283
   PubMed Web of Science ®Google Scholar
• Nalabothula N, Indig FE, Carrier F. The nucleolus takes control of protein trafficking under stress. Mol Cell Pharmacol 2010; 2:203 - 12; PMID: 21499571
   PubMedGoogle Scholar