TPPP/p25: From unfolded protein to misfolding disease: Prediction and experiments

Biology of the Cell

Volumn 96, Issue 9, 2004, Pages 701-711

  Orosz, F ^a   Kovacs G G ^b   Lehotzky, A ^a   Olah J ^a   Vincze, O ^a   Ovadi J ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b NATIONAL INSTITUTE OF PSYCHIATRY AND NEUROLOGY   (Hungary)

Author keywords

Energy state; Intrinsically unstructured proteins; Neurodegeneration

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ADENOSINE TRIPHOSPHATE; ALPHA SYNUCLEIN; GLUCOSE; GLUCOSE 6 PHOSPHATE ISOMERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEXOKINASE; PHOSPHATE; PROTEIN P25; TAU PROTEIN; TRIOSEPHOSPHATE ISOMERASE; TUBULIN; VIMENTIN;

ADULT; AGED; ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ANTIBODY LABELING; ARTICLE; BRAIN TISSUE; CELL CLONE; CELL FREE SYSTEM; CELL INCLUSION; CELL METABOLISM; CELLULAR DISTRIBUTION; CONTROLLED STUDY; DEGENERATIVE DISEASE; ENERGY METABOLISM; ENZYME ACTIVITY; FEMALE; FLUORESCENCE MICROSCOPY; GENETIC TRANSFECTION; GLUCOSE METABOLISM; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; MATHEMATICAL MODEL; MITOCHONDRIAL MEMBRANE; NEUROBLASTOMA CELL; PARKINSON DISEASE; PATHOGENESIS; PATHOPHYSIOLOGY; PREDICTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; SHY DRAGER SYNDROME;

BRAIN; CIRCULAR DICHROISM; GENES, REPORTER; HUMANS; IMMUNOHISTOCHEMISTRY; NERVE TISSUE PROTEINS; NEURODEGENERATIVE DISEASES; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SPECTROMETRY, FLUORESCENCE;

EID: 10244264868     PISSN: 02484900     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biolcel.2004.08.002     Document Type: Article

References (42)

1. M.A. Alim M.S. Hossain K. Arima K. Takeda Y. Izumiyama M. Nakamura et al. Tubulin seeds alpha-synuclein fibril formation J. Biol. Chem. 277 2002 2112-2117
2. E. Beutler K.G. Blume J.C. Kaplan G.W. Löhr B. Ramot W.N. Valentine International Committee for Standardization in Haematology: Recommended methods for red-cell enzyme analysis Br. J. Haematol. 35 1977 331-340
3. M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248-254
4. Y.-H. Chen J.T. Yang H.M. Martinez Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion Biochemistry 11 1972 4120-4131
5. T.J. Collins M.D. Bootman Mitochondria are morphologically heterogeneous within cells J. Exp. Biol. 206 12 2003 1993-2000
6. Z. Dosztányi A. Fiser I. Simon Stabilization centers in proteins: identification, characterization and predictions J. Mol. Biol. 272 1997 597-612
7. A.K. Dunker C.J. Brown J.D. Lawson L.M. Iakoucheva Z. Obradovic Intrinsic disorder and protein function Biochemistry 41 2002 6573-6582
8. A.K. Dunker C.J. Brown Z. Obradovic Identification and functions of usefully disordered proteins Adv. Protein. Chem. 62 2002 25-49
9. A.K. Dunker J.D. Lawson C.J. Brown R.M. Williams P. Romero J.S. Oh et al. Intrinsically disordered protein J. Mol. Graph. Model. 19 2001 26-59
10. H.J. Dyson P.E. Wright Coupling of folding and binding for unstructured proteins Curr. Opin. Struct. Biol. 12 2002 54-60
11. M. Fuxreiter I. Simon P. Friedrich P. Tompa Preformed structural elements feature in partner recognition by intrinsically unstructured proteins J. Mol. Biol. 338 2004 1015-1026
12. M. Goedert Alpha-synuclein and neurodegerative diseases Nat. Rev. Neurosci. 2 2001 492-501
13. E. Hlavanda J. Kovács J. Oláh F. Orosz K.F. Medzihradszky J. Ovádi Brain-specific p25 protein binds to tubulin and microtubules and induces aberrant microtubule assemblies at substoichiometric concentrations Biochemistry 41 2002 8657-8664
14. Q.X. Hua W.H. Jia B.P. Bullock J.F. Habener M.A. Weiss Transcriptional activator-coactivator recognition: Nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding Biochemistry 37 1998 5858-5866
15. T. Iijima T. Mishima K. Akagawa Y. Iwao Mitochondrial hyperpolarization after transient oxygen-glucose deprivation and subsequent apoptosis in cultured rat hippocampal neurons Brain Res. 993 2003 140-145
16. P.H. Jensen H. Hager M.S. Nielsen P. Hojrup J. Gliemann R. Jakes Alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356 J. Biol. Chem. 274 1999 25481-25489
17. P.H. Jensen K. Islam J. Kenney M.S. Nielsen J. Power W.P. Gai Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds alpha-synuclein filaments J. Biol. Chem. 275 2000 21500-21507
18. J.A. Johnston C.L. Ward R.R. Kopito Aggresomes: A cellular response to misfolded proteins J. Cell Biol. 143 1998 1883-1898
19. Kovács G.G. László L. Kovács J. Jensen P.H. Lindersson E. Botond G. Natively unfolded tubulin polymerization promoting protein TPPP/p25 is a common marker of alpha-synucleinopathies Neurobiol. Dis. 17 2004 157-162
20. P. Kurosinski M. Guggisberg J. Götz Alzheimer's and Parkinson's disease - overlapping or synergistic pathologies? Trends Mol. Med. 8 2002 3-5
21. X. Li P. Romero M. Rani A.K. Dunker Z. Obradovic Predicting protein disorder for N-, C-, and internal regions Genome Inform. Ser. Workshop Genome Inform. 10 1999 30-40
22. E. Lindersson R. Beedholm P. Hojrup T. Moos W. Gai K.B. Hendil P.H. Jensen Proteasomal inhibition by alpha-synuclein filaments and oligomers J. Biol. Chem. 279 2004 12924-12934
23. J.L. Mazzola M.A. Sirover Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts J. Neurochem. 76 2001 442-449
24. J.L. Mazzola M.A. Sirover Alteration of intracellular structure and function of glyceraldehyde-3-phosphate dehydrogenase: A common phenotype of neurodegenerative disorders? Neurotoxicology 23 2002 603-609
25. W.A. Meier-Ruge C. Bertoni-Freddari Pathogenesis of decreased glucose turnover and oxidative phosphorylation in ischemic and trauma-induced dementia of the Alzheimer type Ann. N. Y. Acad. Sci. 826 1997 229-241
26. P.J. Mulquiney P.W. Kuchel Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based on detailed enzyme kinetic equations: equations and parameter refinement Biochem. J. 342 1999 581-596
27. F. Orosz G. Wágner F. Ortega M. Cascante J. Ovádi Glucose conversion by multiple pathways in brain extract: Theoretical and experimental analysis Biochem. Biophys. Res. Comm. 309 2002 792-797
28. J. Ovádi F. Orosz S. Hollán Functional aspects of cellular microcompartmentation in the development of neurodegeneration. Mutation induced aberrant protein-protein associations Mol. Cell. Biochem. 256 257 2004 83-93
29. J.E. Payton R.J. Perrin D.F. Clayton J.M. George Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells Brain Res. Mol. Brain Res. 95 2001 138-145
30. R.J. Perrin W.S. Woods D.F. Clayton J.M. George Interaction of human alpha-synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis J. Biol. Chem. 275 2000 34393-34398
31. P. Romero Z. Obradovic X. Li E.C. Garner C.J. Brown A.K. Dunker Sequence complexity of disordered protein Proteins 42 2001 38-48
32. H. Schulze A. Schuyler D. Stuber H. Dobeli H. Langen G. Huber Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein J. Neurochem. 60 1993 1915-1922
33. L.C. Serpell J. Berriman R. Jakes M. Goedert R.A. Crowther Fiber diffraction of synthetic alpha-synuclein filaments show amyloid-like cross-beta conformation Proc. Natl. Acad. Sci. USA 97 2000 4897-4902
34. M. Takahashi K. Tomizawa K. Ishiguro K. Sato A. Omori S. Sato et al. A novel brain-specific 25Da protein (p25) is phosphorylated by a Ser/Thr-Pro kinase (TPK II) from tau protein kinase fractions FEBS Lett. 289 1991 37-43
35. M. Takahashi K. Tomizawa S.C. Fujita K. Sato T. Uchida K. Imahori A brain-specific protein p25 is localized and associated with oligodendrocytes, neuropil, and fiber-like structures of the CA3 hippocampal region in the rat brain J. Neurochem. 60 1993 228-235
36. L. Tirián E. Hlavanda J. Oláh I. Horváth F. Orosz B. Szabó TPPP/p25 promotes tubulin assemblies and blocks mitotic spindle formation Proc. Natl. Acad. Sci. USA 100 2003 13976-13981
37. P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 27 2002 527-533
38. P. Tompa Intrinsically unstructured proteins evolve by repeat expansion Bioessays 25 2003 847-855
39. K. Uéda T. Saitoh H. Mori Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of Alzheimer's disease amyloid Biochem. Biophys. Res. Commun. 205 1994 1366-1372
40. V.N. Uversky Natively unfolded proteins: A point where biology waits for physics Protein Sci. 11 2002 739-756
41. V.N. Uversky J.R. Gillespie A.L. Fink Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41 2001 315-427
42. P.H. Weinreb W. Zhen A.W. Poon K.A. Conway P.T. Lansbury Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded Biochemistry 35 1996 13709-13715