Enhancing protein disaggregation restores proteasome activity in aged cells

Aging

Volumn 5, Issue 11, 2013, Pages 802-812

  Andersson, Veronica ^a   Hanzén, Sarah ^a   Liu, Beidong ^a   Molin, Mikael ^a   Nyström, Thomas ^a  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

Author keywords

Disaggregation; Proteasome; Replicative aging; UPS; Yeast

Indexed keywords

PROTEASOME; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN;

AGING; ARTICLE; CELL AGING; METABOLISM; SACCHAROMYCES CEREVISIAE;

AGING; CELL AGING; PROTEASOME ENDOPEPTIDASE COMPLEX; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN;

EID: 84891529441     PISSN: 19454589     EISSN: None     Source Type: Journal    
DOI: 10.18632/aging.100613     Document Type: Article

References (45)

1. Stadtman ER, Starke-Reed PE, Oliver CN, Carney JM and Floyd RA. Protein modification in aging. Exs. 1992; 62:64-72.
2. Barja G. Mitochondrial free radical production and aging in mammals and birds. Annals of the New York Academy of Sciences. 1998; 854:224-238.
3. Levine RL. Carbonyl modified proteins in cellular regulation, aging, and disease. Free radical biology & medicine. 2002; 32:790-796.
4. Nystrom T. Role of oxidative carbonylation in protein quality control and senescence. The EMBO journal. 2005; 24:1311-1317.
5. Koga H, Kaushik S and Cuervo AM. Protein homeostasis and aging: The importance of exquisite quality control. Ageing research reviews. 2011; 10:205-215.
6. Baraibar MA and Friguet B. Changes of the proteasomal system during the aging process. Progress in molecular biology and translational science. 2012; 109:249-275.
7. Morimoto RI and Cuervo AM. Protein homeostasis and aging: taking care of proteins from the cradle to the grave. The journals of gerontology Series A, Biological sciences and medical sciences. 2009; 64:167-170.
8. Friguet B, Bulteau AL, Chondrogianni N, Conconi M and Petropoulos I. Protein degradation by the proteasome and its implications in aging. Annals of the New York Academy of Sciences. 2000; 908:143-154.
9. Shringarpure R and Davies KJ. Protein turnover by the proteasome in aging and disease. Free radical biology & medicine. 2002; 32:1084-1089.
10. Sitte N, Huber M, Grune T, Ladhoff A, Doecke WD, Von Zglinicki T and Davies KJ. Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts. FASEB journal: official publication of the Federation of American Societies for Experimental Biology. 2000; 14:1490-1498.
11. Zhai Q, Wang J, Kim A, Liu Q, Watts R, Hoopfer E, Mitchison T, Luo L and He Z. Involvement of the ubiquitin-proteasome system in the early stages of wallerian degeneration. Neuron. 2003; 39:217-225.
12. Mizuno Y, Hattori N, Mori H, Suzuki T and Tanaka K. Parkin and Parkinson's disease. Current opinion in neurology. 2001; 14:477-482.
13. Cummings CJ, Reinstein E, Sun Y, Antalffy B, Jiang Y, Ciechanover A, Orr HT, Beaudet AL and Zoghbi HY. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron. 1999; 24:879-892.
14. Fernandez-Funez P, Nino-Rosales ML, de Gouyon B, She WC, Luchak JM, Martinez P, Turiegano E, Benito J, Capovilla M, Skinner PJ, McCall A, Canal I, Orr HT, et al. Identification of genes that modify ataxin-1-induced neurodegeneration. Nature. 2000; 408:101-106.
15. Zabel C, Nguyen HP, Hin SC, Hartl D, Mao L and Klose J. Proteasome and oxidative phoshorylation changes may explain why aging is a risk factor for neurodegenerative disorders. Journal of proteomics. 2010; 73:2230-2238.
16. Kruegel U, Robison B, Dange T, Kahlert G, Delaney JR, Kotireddy S, Tsuchiya M, Tsuchiyama S, Murakami CJ, Schleit J, Sutphin G, Carr D, Tar K, et al. Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiae. PLoS genetics. 2011; 7:e1002253.
17. Vilchez D, Morantte I, Liu Z, Douglas PM, Merkwirth C, Rodrigues AP, Manning G and Dillin A. RPN-6 determines C. elegans longevity under proteotoxic stress conditions. Nature. 2012; 489:263-268.
18. Fredriksson A, Johansson Krogh E, Hernebring M, Pettersson E, Javadi A, Almstedt A and Nystrom T. Effects of aging and reproduction on protein quality control in soma and gametes of Drosophila melanogaster. Aging cell. 2012; 11:634-643.
19. Glover JR and Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 1998; 94:73-82.
20. Eisele F and Wolf DH. Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1. FEBS letters. 2008; 582:4143-4146.
21. Erjavec N, Larsson L, Grantham J and Nystrom T. Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregationremodeling factor Hsp104p. Genes & development. 2007; 21:2410-2421.
22. Russell SJ, Sathyanarayana UG and Johnston SA. Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26 S proteasome. The Journal of biological chemistry. 1996; 271:32810-32817.
23. Xie Y and Varshavsky A. RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Proceedings of the National Academy of Sciences of the United States of America. 2001; 98:3056-3061.
24. Bence NF, Sampat RM and Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 2001; 292:1552-1555.
25. Jana NR, Zemskov EA, Wang G and Nukina N. Altered proteasomal function due to the expression of polyglutamineexpanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Human molecular genetics. 2001; 10:1049-1059.
26. Verhoef LG, Lindsten K, Masucci MG and Dantuma NP. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Human molecular genetics. 2002; 11:2689-2700.
27. Outeiro TF and Lindquist S. Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science. 2003; 302:1772-1775.
28. Holmberg CI, Staniszewski KE, Mensah KN, Matouschek A and Morimoto RI. Inefficient degradation of truncated polyglutamine proteins by the proteasome. The EMBO journal. 2004; 23:4307-4318.
29. Venkatraman P, Wetzel R, Tanaka M, Nukina N and Goldberg AL. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutaminecontaining proteins. Molecular cell. 2004; 14:95-104.
30. Grune T, Jung T, Merker K and Davies KJ. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. The international journal of biochemistry & cell biology. 2004; 36:2519-2530.
31. Hochstrasser M. Ubiquitin-dependent protein degradation. Annual review of genetics. 1996; 30:405-439.
32. Goldberg AL, Stein R and Adams J. New insights into proteasome function: from archaebacteria to drug development. Chemistry & biology. 1995; 2:503-508.
33. Hershko A and Ciechanover A. The ubiquitin system. Annual review of biochemistry. 1998; 67:425-479.
34. Hughes AL and Gottschling DE. An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast. Nature. 2012; 492:261-265.
35. Laun P, Pichova A, Madeo F, Fuchs J, Ellinger A, Kohlwein S, Dawes I, Frohlich KU and Breitenbach M. Aged mother cells of Saccharomyces cerevisiae show markers of oxidative stress and apoptosis. Molecular microbiology. 2001; 39:1166-1173.
36. Molin M, Yang J, Hanzen S, Toledano MB, Labarre J and Nystrom T. Life span extension and H(2)O(2) resistance elicited by caloric restriction require the peroxiredoxin Tsa1 in Saccharomyces cerevisiae. Molecular cell. 2011; 43:823-833.
37. Chondrogianni N, Petropoulos I, Franceschi C, Friguet B and Gonos ES. Fibroblast cultures from healthy centenarians have an active proteasome. Experimental gerontology. 2000; 35:721- 728.
38. Perez VI, Buffenstein R, Masamsetti V, Leonard S, Salmon AB, Mele J, Andziak B, Yang T, Edrey Y, Friguet B, Ward W, Richardson A and Chaudhuri A. Protein stability and resistance to oxidative stress are determinants of longevity in the longestliving rodent, the naked mole-rat. Proceedings of the National Academy of Sciences of the United States of America. 2009; 106:3059-3064.
39. Huh WK, Falvo JV, Gerke LC, Carroll AS, Howson RW, Weissman JS and O'Shea EK. Global analysis of protein localization in budding yeast. Nature. 2003; 425:686-691.
40. Janke C, Magiera MM, Rathfelder N, Taxis C, Reber S, Maekawa H, Moreno-Borchart A, Doenges G, Schwob E, Schiebel E and Knop M. A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast. 2004; 21:947-962.
41. Bachmair A, Finley D and Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science. 1986; 234:179-186.
42. Medicherla B, Kostova Z, Schaefer A and Wolf DH. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO reports. 2004; 5:692-697
43. Smeal T, Claus J, Kennedy B, Cole F and Guarente L. Loss of transcriptional silencing causes sterility in old mother cells of S. cerevisiae. Cell. 1996; 84:633-642.
44. Park SH, Bolender N, Eisele F, Kostova Z, Takeuchi J, Coffino P and Wolf DH. The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum importincompetent proteins to degradation via the ubiquitinproteasome system. Molecular biology of the cell. 2007; 18:153- 165.
45. Kennedy BK, Austriaco NR, Jr. and Guarente L. Daughter cells of Saccharomyces cerevisiae from old mothers display a reduced life span. The Journal of cell biology. 1994; 127:1985-1993