The alternative role of 14-3-3 zeta as a sweeper of misfolded proteins in disease conditions

Medical Hypotheses

Volumn 67, Issue 1, 2006, Pages 169-171

  Kaneko, Kiyotoshi ^a   Hachiya, Naomi S ^a  

^a TOKYO MEDICAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; PROTEIN 14 3 3; PROTEIN 14 3 3 ZETA; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; CELL INCLUSION; CELL NUCLEUS INCLUSION BODY; CELL PROTECTION; CREUTZFELDT JAKOB DISEASE; DIFFUSE LEWY BODY DISEASE; DISEASE ASSOCIATION; HYDROPHOBICITY; MOLECULAR RECOGNITION; NEUROFIBRILLARY TANGLE; NEUROPROTECTION; NEUROTOXICITY; PARKINSON DISEASE; PICK PRESENILE DEMENTIA; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SPINOCEREBELLAR DEGENERATION;

14-3-3 PROTEINS; ANIMALS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HUMANS; MODELS, BIOLOGICAL; NEURODEGENERATIVE DISEASES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN ISOFORMS;

ATAXIA;

EID: 33646097228     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2006.01.019     Document Type: Article

References (20)

1. Berg D., Holzmann C., and Riess O. 14-3-3 proteins in the nervous system. Nat Rev Neurosci 4 (2003) 752-762
2. Lustbader J.W., Cirilli M., Lin C., et al. ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 304 (2004) 448-452
3. Greenamyre J.T., and Hastings T.G. Biomedicine. Parkinson's - divergent causes, convergent mechanisms. Science 304 (2004) 1120-1122
4. Hachiya N.S., Ohkubo T., Kozuka Y., et al. More than a 100-fold increase in immunoblot signals of laser-microdissected inclusion bodies with an excessive aggregation property by oligomeric actin interacting protein 2/d-lactate dehydrogenase protein 2. Anal Biochem 347 (2005) 106-111
5. Mayer M.P., Schroder H., Rudiger S., et al. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat Struct Biol 7 (2000) 586-593
6. Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat Med 10 Suppl. (2004) S10-S17
7. Hashiguchi M., Sobue K., and Paudel H.K. 14-3-3zeta is an effector of tau protein phosphorylation. J Biol Chem 275 (2000) 25247-25254
8. Hernandez F., Cuadros R., and Avila J. Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers. Neurosci Lett 357 (2004) 143-146
9. Umahara T., Uchihara T., Tsuchiya K., et al. 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease. Acta Neuropathol (Berl) 108 (2004) 279-286
10. Umahara T., Uchihara T., Tsuchiya K., et al. Immunolocalization of 14-3-3 isoforms in brains with Pick body disease. Neurosci Lett 371 (2004) 215-219
11. Kawamoto Y., Akiguchi I., Nakamura S., and Budka H. 14-3-3 proteins in Lewy body-like hyaline inclusions in patients with sporadic amyotrophic lateral sclerosis. Acta Neuropathol (Berl) 108 (2004) 531-537
12. Richard M., Biacabe A.G., Streichenberger N., et al. Immunohistochemical localization of 14.3.3 zeta protein in amyloid plaques in human spongiform encephalopathies. Acta Neuropathol (Berl) 105 (2003) 296-302
13. Chen H.K., Fernandez-Funez P., Acevedo S.F., et al. Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1. Cell 113 (2003) 457-468
14. Wiltfang J., Otto M., Baxter H.C., et al. Isoform pattern of 14-3-3 proteins in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. J Neurochem 73 (1999) 2485-2490
15. Kawamoto Y., Akiguchi I., Nakamura S., et al. 14-3-3 proteins in Lewy bodies in Parkinson disease and diffuse Lewy body disease brains. J Neuropathol Exp Neurol 61 (2002) 245-253
16. Liu D., Bienkowska J., Petosa C., et al. Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 376 (1995) 191-194
17. Obsil T., Ghirlando R., Klein D.C., Ganguly S., and Dyda F. Crystal structure of the 14-3-3 zeta:serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation. Cell 105 (2001) 257-267
18. Houry W.A. Mechanism of substrate recognition by the chaperonin GroEL. Biochem Cell Biol 79 (2001) 569-577
19. Tanaka M., Kim Y.M., Lee G., et al. Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. J Biol Chem 279 (2004) 4625-4631
20. Forman M.S., Trojanowski J.Q., and Lee V.M. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat Med 10 (2004) 1055-1063