Regulation of the phosphorylation state and microtubule-binding activity of tau by protein phosphatase 2A

Neuron

Volumn 17, Issue 6, 1996, Pages 1201-1207

  Sontag, Estelle ^a   Nunbhakdi Craig, Viyada ^a   Lee, Gloria ^b   Bloom, George S ^a   Mumby, Marc C ^a  

^a UNIVERSITY OF TEXAS AT DALLAS   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MICROTUBULE ASSOCIATED PROTEIN; PHOSPHOPROTEIN PHOSPHATASE 2A; TAU PROTEIN;

ANIMAL CELL; ARTICLE; CELL STRAIN 3T3; CONTROLLED STUDY; GENETIC TRANSFECTION; MICROTUBULE ASSEMBLY; MONKEY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN POLYMORPHISM; PROTEIN PROTEIN INTERACTION;

EID: 0030461275     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80250-0     Document Type: Article

References (34)

1. Biernat, J., Mandelkow, E.-M., Schroter, C., Lichtenberg-Kraag, B., Steiner, B., Berkling, B., Meyer, H., Mercken, M., Vandermeeren, A., Goedert, M., and Mandelkow, E. (1992). The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region. EMBO J. 11, 1593-1597.
2. Biernat, J., Gustke, N., Drewes, G., Mandelkow, E.-M., and Mandelkow, E. (1993). Phosphorylation of serine 262 strongly reduces the binding of tau protein to microtubules: distinction between PHF-like immunoreactivityand microtubule-binding. Neuron 11, 153-163.
3. Binder, L.I., Frankfurter, A., and Rebhun, L. (1985). The distribution of tau in the normal mammalian nervous system. J. Cell Biol. 101, 1371-1378.
4. 396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 10, 1089-1099.
5. Brandt, R., and Lee, G. (1993). Functional organization of microtubule-associated protein tau: identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro. J. Biol. Chem. 268, 3414-3419.
6. Drewes, G., Mandelkow, E.-M., Baumann, K., Gorris, J., Merlevede, W., and Mandelkow, E. (1993). Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase 2A. FEBS Lett. 336, 425-432.
7. Drubin, D.G., and Kirschner, M.W. (1986). Tau protein function in living cells. J. Cell Biol. 103, 2739-2746.
8. Goedert, M. (1993). Tau protein and the neurofibrillary pathology of Alzheimer's disease. Trends Neurosci. 16, 460-465.
9. Goedert, M., Cohen, E.S., Jakes, R., and Cohen, P. (1992). p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1: implications for Alzheimer's disease. FEBS Lett. 312, 95-99.
10. Goedert, M., Spillantini, M.G., Jakes, R., Crowther, R.A., Vanmechelen, E., Probst, A., Gotz, J., Burki, K., and Cohen, P. (1995a). Molecular dissection of the paired helical filament. Neurobiol. Aging 16, 325-334.
11. Goedert, M., Jakes, R., and Vanmechelen, E. (1995b). Monoclonal antibody AT8 recognizes tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 189, 167-170.
12. Goedert, M., Jakes, R., Wang, J.H., and Cohen, P. (1995c). Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed kinases or cyclic AMP-dependent protein kinase. J. Neurochem. 65, 2804-2807.
13. Gong, C.-X., Singh, T.J., Damuni, Z., and Iqbal, K. (1994). Dephosphorylation of microtubule-associated protein tau by protein phosphatase-1 and -2C and its implication in Alzheimer disease. FEBS Lett. 341, 94-98.
14. Gong, C.-X., Shaikh, S., Wang, J.-Z., Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1995). Phosphatase activity toward abnormally phosphorylated tau: decrease in Alzheimer disease brain. J. Neurochem. 65, 732-738.
15. Greenberg, S.G., Davies, P., Scheim, J.P., and Binder, L.I. (1992). Hydrofluoric acid-treated Τ PHF proteins display the same properties as normal tau. J. Biol. Chem. 267, 564-569.
16. Kamibayashi, C., Estes, R., Slaughter, C., and Mumby, M.C. (1991). Subunit interactions control protein phosphatase 2A: effects of limited proteolysis, N-ethylmaleimide, and heparin on the B subunit. J. Biol. Chem. 266, 13251-13260.
17. Kamibayashi, C., Estes, R., Lickteig, R.L., Yang, S.-I., Craft, C., and Mumby, M.C. (1994). Comparison of heterotrimeric protein phosphatases 2A containing different B subunits. J. Biol. Chem. 269, 20139-20148.
18. Kim, H., Binder, L.I., and Rosenbaum, J.L. (1979). The periodic association of MAP2 with brain microtubules in vitro. J. Cell Biol. 80, 266-276.
19. Lang, E., Szendrei, G.I., Lee, V.M.-Y., and Otvos, L., Jr. (1992). Immunological and conformational characterization of a phosphorylated immunodominant epitope of the paired helical filaments found in Alzheimer's disease. Biochem. Biophys. Res. Commun. 187, 783-790.
20. Lee, G., and Rook, S.L. (1992). Expression of tau in non-neuronal cells: microtubule binding and stabilization. J. Cell Sci. 102, 227-237.
21. Lee, V.M.-Y., Balin, B.J., Otvos, L.J., and Trojanowski, J.Q. (1991). A68: a major subunit of paired helical filaments and derivatized forms of normal tau. Science 251, 675-678.
22. Matsuo, E.S., Shin, R.-W., Billingsley, M.L., Van deVoorde, A., O'Connor, M., Trojanowski, J.Q., and Lee, V.M.-Y. (1994). Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13, 989-1002.
23. Morishima-Kawashima, M., and Kosik, K.S. (1996). The pool of MAP kinase associated with microtubules is small but constitutively active. Mol. Biol. Cell 7, 893-905.
24. 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, 823-829.
25. Mumby, M.C., and Walter, G. (1993). Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth. Physiol. Rev. 73, 673-700.
26. r = 38,000 phosphatase is the catalytic subunit of the native enzyme(s). J. Biol. Chem. 260, 13763-13770.
27. Mumby, M.C., Russell, K.L., Garrard, L.J., and Green, D.D. (1987). Cardiac contractile protein phosphatases: purification of two enzyme forms and their characterization with subunit-specific antibodies. J. Biol. Chem. 262, 6257-6265.
28. Papasozomenos, S.C., and Binder, L.I. (1987). Phosphorylation determines two distinct species of tau in the central nervous system. Cell Motil. Cytoskel. 8, 210-226.
29. Saito, T., Ishiguro, K., Uchida, T., Miyamoto, E., Kishimoto, T., and Hisanaga, S.-I. (1995). In situ dephosphorylation of tau by protein phoshatase 2A and 2B in fetal rat primary cultured neurons. FEBS Lett. 376, 238-242.
30. 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 effects on microtubule assembly. J. Biol. Chem. 268, 1166-1173.
31. Sontag, E., Fedorov, S., Kamibayashi, C., Robbins, R., Cobb, M., and Mumby, M. (1993). The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the MAP kinase pathway and induces cell proliferation. Cell 75, 887-897.
32. Sontag, E., Nunbhakdi-Craig, V., Bloom, G.S., and Mumby, M.C. (1995). A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell-cycle. J. Cell Biol. 128, 1131-1144.
33. Vallee, R.B., and Bloom, G.S. (1983). Isolation of sea urchin egg microtubules with taxol and identification of mitotic spindle microtubule-associated proteins with monoclonal antibodies. Proc. Natl. Acad. Sci. USA 80, 6259-6263.
34. Yamamoto, H., Hasegawa, M., Ono, T., Tashima, K., Ihara, Y., and Eishichi, M. (1995). Dephosphorylation of fetal-tau and paired helical filaments-tau by protein phosphatases 1 and 2A and calcineurin. J. Biochem. 118, 1224-1231.