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Cell Growth and Development

Inactivation of Dual-Specificity Phosphatases Is Involved in the Regulation of Extracellular Signal-Regulated Kinases by Heat Shock and Hsp72

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Pages 3813-3824 | Received 01 Aug 2002, Accepted 03 Mar 2003, Published online: 27 Mar 2023

REFERENCES

  • Alessi, D. R., N. Gomez, G. Moorhead, T. Lewis, S. M. Keyse, and P. Cohen. 1995. Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines. Curr. Biol. 5: 283–295.
  • Camps, M., A. Nichols, C. Gillieron, B. Antonsson, M. Muda, C. Chabert, U. Boschert, and S. Arkinstall. 1998. Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science 280: 1262–1265.
  • Erhardt, P., E. J. Schremser, and G. M. Cooper. 1999. B-Raf inhibits programmed cell death downstream of cytochrome c release from mitochondria by activating the MEK/Erk pathway. Mol. Cell. Biol. 19: 5308–5315.
  • Feige, U., R. Morimoto, I. Yahara, and B. Polla. 1996. Stress-inducible cellular responses. Birkhauser Verlag, Basel, Switzerland.
  • Gabai, V. L., A. B. Meriin, J. A. Yaglom, J. Y. Wei, D. D. Mosser, and M. Y. Sherman. 2000. Suppression of stress kinase JNK is involved in HSP72-mediated protection of myogenic cells from transient energy deprivation. HSP72 alleviates the stress-induced inhibition of JNK dephosphorylation. J. Biol. Chem. 275: 38088–38094.
  • Gabai, V. L., A. B. Meriin, D. D. Mosser, A. W. Caron, S. Rits, V. I. Shifrin, and M. Y. Sherman. 1997. HSP70 prevent activation of stress kinases: a novel pathway of cellular thermotolerance. J. Biol. Chem. 272: 18033–18037.
  • Gabai, V. L., and M. Y. Sherman. 2002. Invited review: interplay between molecular chaperones and signaling pathways in survival of heat shock. J. Appl. Physiol. 92: 1743–1748.
  • Gabai, V. L., J. A. Yaglom, V. Volloch, A. B. Meriin, T. Force, M. Koutroumanis, B. Massie, D. D. Mosser, and M. Y. Sherman. 2000. Hsp72-mediated suppression of c-Jun N-terminal kinase is implicated in development of tolerance to caspase-independent cell death. Mol. Cell. Biol. 20: 6826–6836.
  • Gossen, M., and H. Bujard. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89: 5547–5551.
  • Groom, L. A., A. A. Sneddon, D. R. Alessi, S. Dowd, and S. M. Keyse. 1996. Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase. EMBO J. 15: 3621–3632.
  • Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381: 571–579.
  • Holmstrom, T. H., S. E. Tran, V. L. Johnson, N. G. Ahn, S. C. Chow, and J. E. Eriksson. 1999. Inhibition of mitogen-activated kinase signaling sensitizes HeLa cells to Fas receptor-mediated apoptosis. Mol. Cell. Biol. 19: 5991–6002.
  • Jani, A., H. Lochmuller, G. Acsadi, M. Simoneau, J. Huard, A. Garnier, G. Karpati, and B. Massie. 1997. Generation, validation, and large scale production of adenoviral recombinants with large size inserts such as a 6.3-kb human dystrophin cDNA. J. Virol. Methods 64: 111–124.
  • Keyse, S. M. 1998. Protein phosphatases and the regulation of MAP kinase activity. Semin. Cell. Dev. Biol. 9: 143–152.
  • Keyse, S. M., and E. A. Emslie. 1992. Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase. Nature 359: 644–647.
  • Kyriakis, J. M. 1999. Making the connection: coupling of stress-activated ERK/MAPK (extracellular-signal-regulated kinase/mitogen-activated protein kinase) core signalling modules to extracellular stimuli and biological responses. Biochem. Soc. Symp. 64: 29–48.
  • Liossis, S.-N. C., X. Z. Ding, J. G. Kiang, and G. C. Tsokos. 1997. Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells. J. Immunol. 158: 5668–5675.
  • Massie, B., F. Couture, L. Lamoureux, D. D. Mosser, C. Guilbault, P. Jolicoeur, F. Belanger, and Y. Langelier. 1998. Inducible overexpression of a toxic protein by an adenovirus vector with a tetracycline-regulatable expression cassette. J. Virol. 72: 2289-2296.
  • Meriin, A. B., J. A. Yaglom, V. L. Gabai, D. D. Mosser, L. Zon, and M. Y. Sherman. 1999. Protein damaging stresses activate JNK via inhibition of its phosphatase: a novel pathway controlled by Hsp72. Mol. Cell. Biol. 19: 2547–2555.
  • Millward, T. A., S. Zolnierowicz, and B. A. Hemmings. 1999. Regulation of protein kinase cascades by protein phosphatase 2A. Trends Biochem. Sci. 24: 186–191.
  • Mosser, D. D., A. W. Caron, L. Bourget, C. Denis-Larose, and B. Massie. 1997. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 17: 5317–5327.
  • Mosser, D. D., A. W. Caron, L. Bourget, P. Jolicoeur, and B. Massie. 1997. Use of a dicistronic expression cassette encoding the green fluorescent protein for the screening and selection of cells expressing inducible gene products. BioTechniques 22: 150–161.
  • Palacios, C., M. K. Collins, and G. R. Perkins. 2001. The JNK phosphatase M3/6 is inhibited by protein-damaging stress. Curr. Biol. 11: 1439–1443.
  • Park, H. S., S. G. Cho, C. K. Kim, H. S. Hwang, K. T. Noh, M. S. Kim, S. H. Huh, M. J. Kim, K. Ryoo, E. K. Kim, W. J. Kang, J. S. Lee, J. S. Seo, Y. G. Ko, S. Kim, and E. J. Choi. 2002. Heat shock protein hsp72 is a negative regulator of apoptosis signal-regulating kinase 1. Mol. Cell. Biol. 22: 7721–7730.
  • Pirkkala, L., P. Nykanen, and L. Sistonen. 2001. Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J. 15: 1118–1131.
  • Saxena, M., and T. Mustelin. 2000. Extracellular signals and scores of phosphatases: all roads lead to MAP kinase. Semin. Immunol. 12: 387–396.
  • Schaeffer, H. J., A. D. Catling, S. T. Eblen, L. S. Collier, A. Krauss, and M. J. Weber. 1998. MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade. Science 281: 1668–1671.
  • Scheid, M. P., and V. Duronio. 1998. Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/Akt: involvement of MEK upstream of Bad phosphorylation. Proc. Natl. Acad. Sci. USA 95: 7439–7444.
  • Song, J., M. Takeda, and R. I. Morimoto. 2001. Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Nat. Cell Biol. 3: 276–282.
  • Strasser, A., and R. L. Anderson. 1995. Bcl-2 and thermotolerance cooperate in cell survival. Cell Growth Differ. 6: 799–805.
  • Tran, S. E., T. H. Holmstrom, M. Ahonen, V. M. Kahari, and J. E. Eriksson. 2001. MAPK/ERK overrides the apoptotic signaling from Fas, TNF, and TRAIL receptors. J. Biol. Chem. 276: 16484–16490.
  • Verheij, M., R. Bose, X. H. Lin, B. Yao, W. D. Jarvis, S. Grant, M. J. Birrer, E. Szabo, L. I. Zon, J. M. Kyriakis, A. Haimovitz-Friedman, Z. Fuks, and R. N. Kolesnick. 1996. Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis. Nature 380: 75–79.
  • Volloch, V. Z., V. L. Gabai, S. Ritz, and M. Y. Sherman. 2000. Hsp72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK. Cell Stress Chaperones 5: 139–147.
  • Weinstein-Oppenheimer, C. R., W. L. Blalock, L. S. Steelman, F. Chang, and J. A. McCubrey. 2000. The Raf signal transduction cascade as a target for chemotherapeutic intervention in growth factor-responsive tumors. Pharmacol. Ther. 88: 229–279.
  • Woessmann, W., Y. H. Meng, and N. F. Mivechi. 1999. An essential role for mitogen-activated protein kinases, ERKs, in preventing heat-induced cell death. J. Cell Biochem. 74: 648–662.

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