Neurodegeneration-Associated Protein Fragments as Short-Lived Substrates of the N-End Rule Pathway

Molecular Cell

Volumn 50, Issue 2, 2013, Pages 161-171

  Brower, Christopher S ^a   Piatkov, Konstantin I ^a   Varshavsky, Alexander ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN[1-42]; ARGININE; TAR DNA BINDING PROTEIN; TAU PROTEIN;

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DEGENERATIVE DISEASE; FIBROBLAST; HUMAN; HUMAN TISSUE; MOUSE; NEUROFIBRILLARY TANGLE; NONHUMAN; PROTEIN DEGRADATION; PROTEIN EXPRESSION; SACCHAROMYCES CEREVISIAE;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; ANIMALS; ARGININE; BRAIN; CALPAIN; CELL EXTRACTS; DNA-BINDING PROTEINS; FRONTOTEMPORAL LOBAR DEGENERATION; HALF-LIFE; HEK293 CELLS; HUMANS; MATRIX METALLOPROTEINASE 3; MICE; MICE, TRANSGENIC; MOLECULAR SEQUENCE DATA; NEURODEGENERATIVE DISEASES; NIH 3T3 CELLS; PEPTIDE FRAGMENTS; PROTEIN STABILITY; PROTEOLYSIS; RETICULOCYTES; SACCHAROMYCES CEREVISIAE; TAU PROTEINS;

MUS;

EID: 84876832401     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2013.02.009     Document Type: Article

References (39)

1. Balch W.E., Morimoto R.I., Dillin A., Kelly J.W. Adapting proteostasis for disease intervention. Science 2008, 319:916-919.
2. Brower C.S., Varshavsky A. Ablation of arginylation in the mouse N-end rule pathway: loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations. PLoS ONE 2009, 4:e7757.
3. Chen B., Retzlaff M., Roos T., Frydman J. Cellular strategies of protein quality control. Cold Spring Harb. Perspect. Biol. 2011, 3:a004374.
4. Choi D.H., Kim Y.J., Kim Y.G., Joh T.H., Beal M.F., Kim Y.S. Role of matrix metalloproteinase 3-mediated alpha-synuclein cleavage in dopaminergic cell death. J. Biol. Chem. 2011, 286:14168-14177.
5. Cremades N., Cohen S.I., Deas E., Abramov A.Y., Chen A.Y., Orte A., Sandal M., Clarke R.W., Dunne P., Aprile F.A., et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 2012, 149:1048-1059.
6. Dawson T.M., Ko H.S., Dawson V.L. Genetic animal models of Parkinson's disease. Neuron 2010, 66:646-661.
7. Dougan D.A., Micevski D., Truscott K.N. The N-end rule pathway: from recognition by N-recognins, to destruction by AAA+proteases. Biochim. Biophys. Acta 2011, 1823:83-91.
8. Eisenberg D., Jucker M. The amyloid state of proteins in human diseases. Cell 2012, 148:1188-1203.
9. Furukawa Y., Kaneko K., Nukina N. Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site. Biochim. Biophys. Acta 2011, 1812:1577-1583.
10. Gabius H.-J., Graupner G., Cramer F. Activity patterns of aminoacyl-tRNA synthetases, tRNA methylases, arginyltransferase and tubulin: tyrosine ligase during development and ageing of Caenorhabditis elegans. Eur. J. Biochem. 1983, 131:231-234.
11. Garg S., Timm T., Mandelkow E.M., Mandelkow E., Wang Y. Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment. Neurobiol. Aging 2011, 32:1-14.
12. Graciet E., Wellmer F. The plant N-end rule pathway: structure and functions. Trends Plant Sci. 2010, 15:447-453.
13. Green D.R. Means to an End: Apoptosis and Other Cell Death Mechanisms 2011, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
14. Huang Y., Mucke L. Alzheimer mechanisms and therapeutic strategies. Cell 2012, 148:1204-1222.
15. Hwang C.-S., Shemorry A., Varshavsky A. N-terminal acetylation of cellular proteins creates specific degradation signals. Science 2010, 327:973-977.
16. Igaz L.M., Kwong L.K., Chen-Plotkin A., Winton M.J., Unger T.L., Xu Y., Neumann M., Trojanowski J.Q., Lee V.M. Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies. J. Biol. Chem. 2009, 284:8516-8524.
17. Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000, 10:524-530.
18. Lagier-Tourenne C., Polymenidou M., Cleveland D.W. TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet. 2010, 19(R1):R46-R64.
19. Lee E.B., Lee V.M., Trojanowski J.Q. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat. Rev. Neurosci. 2012, 13:38-50.
20. Levin J., Giese A., Boetzel K., Israel L., Högen T., Nübling G., Kretzschmar H., Lorenzl S. Increased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinases. Exp. Neurol. 2009, 215:201-208.
21. Lindquist S.L., Kelly J.W. Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb. Perspect. Biol. 2011, 3:a004507.
22. Manczak M., Anekonda T.S., Henson E., Park B.S., Quinn J., Reddy P.H. Mitochondria are a direct site of A beta accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum. Mol. Genet. 2006, 15:1437-1449.
23. Mogk A., Schmidt R., Bukau B. The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol. 2007, 17:165-172.
24. Nonaka T., Kametani F., Arai T., Akiyama H., Hasegawa M. Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum. Mol. Genet. 2009, 18:3353-3364.
25. Oakley H., Cole S.L., Logan S., Maus E., Shao P., Craft J., Guillozet-Bongaarts A., Ohno M., Disterhoft J., Van Eldik L., et al. Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J. Neurosci. 2006, 26:10129-10140.
26. Pesiridis G.S., Tripathy K., Tanik S., Trojanowski J.Q., Lee V.M. A " two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport. J. Biol. Chem. 2011, 286:18845-18855.
27. Piatkov K.I., Brower C.S., Varshavsky A. The N-end rule pathway counteracts cell death by destroying proapoptotic protein fragments. Proc. Natl. Acad. Sci. USA 2012, 109:E1839-E1847.
28. Prusiner S.B. A unifying role for prions in neurodegenerative diseases. Science 2012, 336:1511-1513.
29. Rochet J.C., Hay B.A., Guo M. Molecular insights into Parkinson's disease. Prog. Mol. Biol. Transl. Sci. 2012, 107:125-188.
30. Selkoe D.J. Alzheimer's disease. Cold Spring Harb. Perspect. Biol. 2011, 3:a004457.
31. Serrano-Pozo A., Frosch M.P., Masliah E., Hyman B.T. Neuropathological alterations in Alzheimer disease. Cold Spring Harb. Perspect. Med. 2011, 1:a006189.
32. Spires-Jones T.L., Kopeikina K.J., Koffie R.M., de Calignon A., Hyman B.T. Are tangles as toxic as they look?. J. Mol. Neurosci. 2011, 45:438-444.
33. Tasaki T.S., Sriram S.M., Park K.S., Kwon Y.T. The N-end rule pathway. Annu. Rev. Biochem. 2012, 81:261-289.
34. Vabulas R.M., Raychaudhuri S., Hayer-Hartl M., Hartl F.U. Protein folding in the cytoplasm and the heat shock response. Cold Spring Harb. Perspect. Biol. 2010, 2:a004390.
35. Varshavsky A. Ubiquitin fusion technique and related methods. Methods Enzymol. 2005, 399:777-799.
36. Varshavsky A. Discovery of cellular regulation by protein degradation. J. Biol. Chem. 2008, 283:34469-34489.
37. Varshavsky A. The N-end rule pathway and regulation by proteolysis. Protein Sci. 2011, 20:1298-1345.
38. Varshavsky A. Augmented generation of protein fragments during wakefulness as the molecular cause of sleep: a hypothesis. Protein Sci. 2012, 21:1634-1661.
39. Vendruscolo M., Knowles T.P., Dobson C.M. Protein solubility and protein homeostasis: a generic view of protein misfolding disorders. Cold Spring Harb. Perspect. Biol. 2011, 3:a010454.