Hsp90 maintains the stability and function of the tau phosphorylating kinase GSK3β

International Journal of Molecular Sciences

Volumn 8, Issue 1, 2007, Pages 51-60

  Dou, Fei ^a   Chang, Xingya ^a   Ma, Da ^a  

^a MEDICAL SCHOOL OF SOUTHEAST UNIVERSITY   (China)

Author keywords

Aberrant tau phosphorylation; GSK3 ; Hsp90; Tauopathy

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3BETA; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEASOME; TAU PROTEIN;

ALZHEIMER DISEASE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME PHOSPHORYLATION; ENZYME STABILITY; NEUROFIBRILLARY TANGLE; NONHUMAN; PATHOGENESIS; RAT;

RATTUS;

EID: 33947325652     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/i8010060     Document Type: Article

References (37)

1. Hartl, F.U. and M. Hayer-Hartl, Molecular chaperones in the cytosol: from nascent chain to folded protein. Science, 2002, 295(5561), 1852-1858.
2. Young, J.C., et al., Pathways of chaperone-mediated protein folding in the cytosol. Nat Rev Mol Cell Biol, 2004, 5(10), 781-791.
3. Goldberg, A.L., Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 426(6968), 895-899.
4. Muchowski, P.J., Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron 2002, 35(1), 9-12.
5. Sherman, M.Y. and A.L. Goldberg, Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 2001, 29(1), 15-32.
6. Muchowski, P.J. and J.L. Wacker, Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 2005, 6(1), 11-22.
7. Slavotinek AM, Biesecker LG. Unfolding the role of chaperones and chaperonins in human disease. Trends Genet. 2001, 17(9), 528-535.
8. Carmichael J, Chatellier J, Woolfson A, Milstein C, Fersht AR, Rubinsztein DC. Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease. Proc. Natl. Acad. Sci. USA 2000, 97(17), 9701-9705.
9. Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, Bonini NM. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet. 1999, 23(4), 425-428.
10. Sittler A, Lurz R, Lueder G, Priller J, Lehrach H, Hayer-Hartl MK, Hartl FU, Wanker EE. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 2001, 10(16), 1307-1315.
11. Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 2002, 295(5556), 865-868.
12. Muchowski PJ, Schaffar G, Sittler A, Wanker EE, Hayer-Hartl MK, Hartl FU. Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proc. Natl. Acad. Sci. USA 2000, 97(14), 7841-7846.
13. Dou F, Netzer WJ, Tanemura K, Li F, Hartl FU, Takashima A, Gouras GK et al. Chaperones increase association of tau protein with microtubules. Proc. Natl. Acad. Sci. USA 2003, 100(2), 721-726.
14. Xu W, Mimnaugh E, Rosser MF, Nicchitta C, Marcu M, Yarden Y, Neckers L. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J. Biol. Chem. 2001, 276(5), 3702-3708.
15. Sato S, Fujita N, Tsuruo T. Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl Acad. Sci. USA 2000, 97(20), 10832-10837.
16. Schulte TW, Blagosklonny MV, Ingui C, Neckers L. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J. Biol. Chem. 1995, 270(41), 24585-24588.
17. de Carcer G, do Carmo Avides M, Lallena MJ, Glover DM, Gonzalez C. Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability. Eur. Mol. Biol. Org. J. 2001, 20 (11), 2878-2884.
18. Dou, F., L.D. Yuan, and J.J. Zhu, Heat shock protein 90 indirectly regulates ERK activity by affecting Raf protein metabolism. Acta Biochim Biophys Sin (Shanghai) 2005, 37(7), 501-505.
19. Vilenchik, M. et al. Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90. Chem. Biol. 2004, 11, 787-797.
20. Xu, H., et al., Estrogen reduces neuronal generation of Alzheimer beta-amyloid peptides. Nat Med 1998, 4(4), 447-51.
21. Lee, V.M., M. Goedert, and J.Q. Trojanowski, Neurodegenerative tauopathies, in Annu Rev Neurosci 2001, 1121-1159.
22. Billingsley, M.L. and R.L. Kincaid, Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem J 1997, 323 ( Pt 3), 577-91.
23. Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 1998, 94(4), 471-480.
24. Singh, T. J., Zaidi, T., Grundke-Iqbal, I. & Iqbal, K. Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-prolinedependent protein kinases. FEBS Lett. 1995, 358, 4-8.
25. Mimnaugh, E., Chavany, C. & Neckers, L. M. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 1996, 271, 22796-22801.
26. Goldbaum, O. and C. Richter-Landsberg, Proteolytic stress causes heat shock protein induction, tau ubiquitination, and the recruitment of ubiquitin to tau-positive aggregates in oligodendrocytes in culture. J Neurosci 2004, 24(25), 5748-5757.
27. Iqbal K, Grundke-Iqbal I. Inhibition of neurofibrillary degeneration: a promising approach to Alzheimer's disease and other tauopathies. Curr Drug Targets 2004, 5(6), 495-502.
28. Stoothoff WH, Johnson GV. Tau phosphorylation: physiological and pathological consequences. Biochim Biophys Acta 2005, Jan 3 1739(2-3), 280-297.
29. Monaco EA 3rd, Vallano ML. Role of protein kinases in neurodegenerative disease: cyclin-dependent kinases in Alzheimer's disease. Front Biosci. 2005, Jan 1 10, 143-159.
30. Kosik, K. S. & Shimura, H. Phosphorylated tau and the neurodegenerative foldopathies. Biochim. Biophys. Acta. 2005, 1739, 298-310.
31. Sang, H. et al. Phosphorylation of tau by glycogen synthase kinase 3β in intact mammalian cells influences the stability of microtubules. Neurosci. Lett. 2001, 312, 141-144.
32. Pei, J.J. et al. Distribution of active glycogen synthase kinase 3β (GSK-3β) in brains staged for Alzheimer disease neurofibrillary changes. J. Neuropathol. Exp. Neurol. 1999, 58, 1010-1019.
33. Yamaguchi, H. et al. Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 β and cyclin-dependent kinase 5, a component of TPK II. Acta Neuropathol. 1996, 92, 232-241.
34. Neckers, L. Chaperoning oncogenes: Hsp90 as a target of geldanamycin. Handb. Exp. Pharmacol. 2006, 172, 259-77.
35. McDonald, E., Workman, P. & Jones, K. Inhibitors of the HSP90 molecular chaperone: attacking the master regulator in cancer. Curr. Top. Med. Chem. 2006, 6, 1091-1107.
36. Chiosis, G. Targeting chaperones in transformed systems - a focus on Hsp90 and cancer. Expert Opin. Ther. Targets 2006, 10, 37-50.
37. Noble W, Planel E, Zehr C, Olm V, Meyerson J, Suleman F, Gaynor K, Wang L, LaFrancois J, Feinstein B, Burns M, Krishnamurthy P, Wen Y, Bhat R, Lewis J, Dickson D, Duff K. Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo. Proc Natl Acad Sci U S A 2005,102(19), 6990-6995.