SEARCH

SEARCH BY CITATION

References

  • Alonso A., Del C., Zaidi T., Grundke-Iqbal I. and Iqbal K. (1994) Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc. Natl Acad. Sci. USA 91, 55625566.
  • Alonso A., Del C., Zaidi T., Novak M., Grundke-Iqbal I. and Iqbal K. (2001) Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc. Natl Acad. Sci. USA 98, 69236928.
  • Andorfer C. A. and Davies P. (2000) PKA phosphorylations on tau: developmental studies in the mouse. Dev. Neurosci. 22, 303309.
  • Avila J., Lim F., Moreno F., Belmonte C. and Cuello A. C. (2002) Tau function and dysfunction in neurons: its role in neurodegenerative disorders. Mol. Neurobiol. 25, 213231.
  • Avila J., Lucas J. J., Perez M. and Hernandez F. (2004) Role of tau protein in both physiological and pathological conditions. Physiol. Rev. 84, 361384.
  • Berg D., Holzman C. and Riess O. (2003) 14-3-3 proteins in the nervous system. Nat. Rev. Neurosci. 4, 752762.
  • Bramblett G. T., Goedert M., Jakes R., Merrick S. E., Trojanowski J. Q. and Lee V. M. (1993) Abnormal tau phosphorylation at Ser396 in Alzheimer’s disease recapitulates development and contributes to reduced microtubule binding. Neuron 10, 10891099.
  • Brion J.-P., Octave J. N. and Couck A. M. (1994) Distribution of the phosphorylated microtubule-associated protein tau in developing cortical neurons. Neuroscience 62, 895909.
  • Buée L., Bussiere T., Buee-Scherrer V., Delacourte A. and Hof P. R. (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res. Brain Res. Rev. 33, 95130.
  • Chun J., Kwon T., Lee E. J., Kim C. H., Han Y. S., Hong S. K., Hyun S. and Kang S. S. (2004) 14-3-3 Protein mediates phosphorylation of microtubule-associated protein tau by serum- and glucocorticoid-induced protein kinase 1. Mol. Cells 18, 360368.
  • Drewes G., Trinczek B., Illenberger S., Biernat J., Schmitt-Ulms G., Meyer H. E., Mandelkow E.-M. and Mandelkow E. (1995) Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau–microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. J. Biol. Chem. 270, 76797688.
  • Freed E., Symons M., Macdonald S. G., McCormick F. and Ruggieri R. C. (1994) Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265, 17131719.
  • Fu H., Subramanian R. R. and Masters S. C. (2000) 14-3-3 proteins: structure, function, and regulation. Annu. Rev. Pharmacol. Toxicol. 40, 617647.
  • Goedert M. and Jakes R. (1990) Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 9, 42254230.
  • Goedert M., Spillantini M. G., Jakes R., Rutherford D. and Crowther R. A. (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer’s disease. Neuron 3, 519526.
  • Goedert M., Jakes R., Crowther R. A., Six J., Lubke U., Vandermeeren M., Cras P., Trojanowski J. Q. and Lee V. M. (1993) The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development. Proc. Natl Acad. Sci. USA 90, 50665070.
  • Goedert M., Jakes R., Spillantini M. G., Hasegawa M., Smith M. J. and Crowther R. A. (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383, 550553.
  • Hanger D. P., Byers H., Wray S., Leung K.-Y., Saxton M. J., Seereeram A., Reynolds C. H., Ward M. A. and Anderton B. H. (2007) Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J. Biol. Chem. 282, 2364523654.
  • Hashiguchi M., Sobue K. and Paudel H. K. (2000) 14-3-3 zeta is an effector of tau protein phosphorylation. J. Biol. Chem. 275, 2524725254.
  • Hernandez F., Cuadors R. and Avila J. (2004) Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers. Neurosci. Lett. 357, 143146.
  • Illenberger S., Zheng-Fischhofer Q., Preuss U., Stamer K., Baumann K., Trinczek B., Biernat J., Godeman R., Mandelkow E.-V. and Mandelkow E. (1998) The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer’s disease. Mol. Biol. Cell 9, 14951512.
  • Iqbal K., Alonso A., Del C. et al. (2005) Tau pathology in Alzheimer disease and other tauopathies. Biochim. Biophys. Acta 1739, 198210.
  • Jicha G. A., Weaver C., Lane E., Vianna C., Kress Y., Rockwood J. and Davies P. (1999) cAMP-dependent protein kinase phosphorylations on tau in Alzheimer’s disease. J. Neurosci. 19, 74867494.
  • Johnson G. V. and Stoothoff W. (2004) Tau phosphorylation in neuronal cell function and dysfunction. J. Cell Sci. 117, 57215729.
  • Kampers T., Friedhoff P., Biernat J., Mandelkow E.-M. and Mandelkow E. (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett. 399, 344349.
  • Kopke E., Tung Y.-C., Shaikh S., Alonso A. C., Iqbal K. and Grundke-Iqbal I. (1993) Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268, 2437424384.
  • Ksiezak-Reding H., Pyo H. K., Feinstein B. and Pasinetti G. M. (2003) Akt/PKB kinase phosphorylates separately Thr212 and Ser214 of tau protein in vitro. Biochim. Biophys. Acta 1639, 159168.
  • Layfield R., Fergusson J., Aitken A., Lowe J., Landon M. and Mayer R. J. (1996) Neurofibrillary tangles of Alzheimer’s disease brains contain 14-3-3 proteins. Neurosci. Lett. 209, 5760.
  • Leger J., Kempf M., Lee G. and Brandt R. (1997) Conversion of serine to aspartate imitates phosphorylation-induced changes in the structure and function of microtubule-associated protein tau. J. Biol. Chem. 272, 84418446.
  • Lu P. J., Wulf G., Zhou X. Z., Davies P. and Lu K. P. (1999) The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399, 784788.
  • Mandelkow E.-M. and Mandelkow E. (1998) Tau in Alzheimer’s disease. Trends Cell Biol. 8, 425427.
  • Morishima-Kawashima M., Hasegawa M., Takio K., Suzuki M., Yoshida H., Titani K. and Ihara Y. (1995) Proline-directed and non-proline-directed phosphorylation of PHF-tau. J. Biol. Chem. 270, 823829.
  • Muslin A. J., Tanner J. W., Allen P. M. and Shaw A. S. (1996) Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3. Cell 84, 889889.
  • Pei J. J., Khatoon S., An W. L. et al. (2003) Role of protein kinase B in Alzheimer's neurofibrillary pathology. Acta Neuropathol. (Berl.) 105, 381392.
  • Perez M., Valpuesta J. M., Medina M., Montejo de Garcini E. and Avila J. (1996) Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau–tau interaction. J. Neurochem. 67, 11831190.
  • Pyo K. H., Lovati E., Pasinetti G. M. and Ksiezak-Reding H. (2004) Phosphorylation of tau at THR212 and SER214 in human neuronal and glial cultures: the role of AKT. Neuroscience 127, 649658.
  • Reuther G. W. and Pendergast A. (1996) The roles of 14-3-3 proteins in signal transduction. Vitam. Horm. 52, 149175.
  • Schneider A., Biernet J., Von Bergen M., Mandelkow E. and Mandelkow E. M. (1998) Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38, 35493558.
  • Scott C. W., Spreen R. C., Herman J. L., Chow F. P., Davison M. D., Young J. and Caputo C. B. (1993) Phosphorylation of recombinant tau by cAMP-dependent protein kinase. Identification of phosphorylation sites and effect on microtubule assembly. J. Biol. Chem. 268, 11661172.
  • Seubert P., Mawal-Dewan M., Barbour R. et al. (1995) Detection of phosphorylated Ser262 in fetal tau, adult tau, and paired helical filament tau. J. Biol. Chem. 270, 1891718922.
  • Shimura H., Miura-Shimura Y. and Kosik K. S. (2004) Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival. J. Biol. Chem. 279, 1795717962.
  • Tanaka T., Iqbal K., Gurundke-Iqbal I., Takeda M. and Nishimura T. (1995a) Dysregulation of phosphorylation system in Alzheimer’s system. Ann. Psychiat. 5, 6579.
  • Tanaka T., Iqbal K., Trenkner E., Liu D. J. and Grundke-Iqbal I. (1995b) Abnormally phosphorylated tau in SY5Y human neuroblastoma cells. FEBS Lett. 360, 59.
  • Tanaka T., Zhong J., Iqbal K., Trenkner E. and Grundke-Iqbal I. (1998) The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: the role of protein phosphatases. FEBS Lett. 426, 248254.
  • Tanaka T., Wada K., Yamamori H. and Takeda M. (2003) Phosphorylation of tau protein at Ser214 induced by lithium. Abstract page no. 38, The 6th international Conference AD/PD, Seville, Spain.
  • Umahara T., Uchihara T., Tsuchiya K., Nakamura A., Iwamoto T., Ikeda K. and Takasaki M. (2004) 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer’s disease. Acta Neuropathol. (Berl.) 108, 279286.
  • Virdee K., Yoshida H., Peak-Chew S. and Goedert M. (2007) Phosphorylation of human microtubule-associated protein tau by protein kinases of the AGC subfamily. FEBS Lett. 581, 26572662.
  • Watanabe A., Hasegawa M., Suzuki M., Takio K., Morishima-Kawashima M., Titani K., Arai T., Kosik K. S. and Ihara Y. (1993) In vivo phosphorylation sites in fetal and adult rat tau. J. Biol. Chem. 268, 2571225717.
  • Yaffe M. B., Rittinger K., Volinia S., Caron P. R., Aitken A., Leffers H., Gamblin S. J., Smerdon S. J. and Cantley L. C. (1997) The structural basis for 14-3-3: phosphopeptide binding specificity. Cell 91, 961971.
  • Yang C. Y., Lin C. H. and Lee E. H. Y. (2006) Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite formation through microtubule depolymerization by SGK1 and by SGK1 phosphorylation of tau. Mol. Cell. Biol. 26, 83578370.
  • Zha J., Harada H., Yang E., Jockel J. and Korsmeyer S. J. (1996) Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87, 619628.