Life-span extension by a metacaspase in the yeast Saccharomyces cerevisiae

Science

Volumn 344, Issue 6190, 2014, Pages 1389-1392

  Hill, Sandra Malmgren ^a   Hao, Xinxin ^a   Liu, Beidong ^a   Nyström, Thomas ^a  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; FUNGAL ENZYME; HEAT SHOCK PROTEIN 104; METACASPASE; UNCLASSIFIED DRUG; CASPASE; CYSTEINE; HEAT SHOCK PROTEIN; HSP104 PROTEIN, S CEREVISIAE; MCA1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

APOPTOSIS; CATALYSIS; ENZYME ACTIVITY; GENE EXPRESSION; GENETIC ANALYSIS; PROTEIN; QUALITY CONTROL; YEAST;

AGING; ARTICLE; GENE INTERACTION; LIFE EXTENSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN HOMEOSTASIS; PROTEIN UNFOLDING; QUALITY CONTROL; SACCHAROMYCES CEREVISIAE; APOPTOSIS; CATALYSIS; CHEMISTRY; ENZYME ACTIVE SITE; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETICS; LONGEVITY; METABOLISM; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PROTEIN DEGRADATION; PROTEIN TRANSPORT; UNFOLDED PROTEIN RESPONSE;

SACCHAROMYCES CEREVISIAE;

APOPTOSIS; CASPASES; CATALYSIS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CYSTEINE; GENE EXPRESSION REGULATION, FUNGAL; HEAT-SHOCK PROTEINS; LONGEVITY; PROTEIN TRANSPORT; PROTEOLYSIS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TRANSCRIPTION, GENETIC; UNFOLDED PROTEIN RESPONSE;

EID: 84902666176     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1252634     Document Type: Article

References (33)

1. J. Yuan, H. R. Horvitz, Cell 116, (Suppl), S53-S56 (2004).
2. E. S. Alnemri et al., Cell 87, 171 (1996).
3. N. N. Danial, S. J. Korsmeyer, Cell 116, 205-219 (2004).
4. P. K. Gregersen, N. Engl. J. Med. 356, 1263-1266 (2007).
5. A. G. Uren et al., Mol. Cell 6, 961-967 (2000).
6. F. Madeo et al., Mol. Cell 9, 911-917 (2002).
7. E. Herker et al., J. Cell Biol. 164, 501-507 (2004).
8. F. Madeo, E. Fröhlich, K. U. Fröhlich, J. Cell Biol. 139, 729-734 (1997).
9. A. Shrestha, L. A. Megeney, Front. Oncol. 2, 78 (2012).
10. R. E. Lee, L. G. Puente, M. Kaern, L. A. Megeney, PLOS One 3, e2956 (2008).
11. R. E. Lee, S. Brunette, L. G. Puente, L. A. Megeney, Proc. Natl. Acad. Sci. U.S.A. 107, 13348-13353 (2010).
12. A. Shrestha, L. G. Puente, S. Brunette, L. A. Megeney, J. Proteomics 81, 24-30 (2013).
13. A. Szallies, B. K. Kubata, M. Duszenko, FEBS Lett. 517, 144-150 (2002).
14. F. U. Hartl, M. Hayer-Hartl, Nat. Struct. Mol. Biol. 16, 574-581 (2009).
15. H. Aguilaniu, L. Gustafsson, M. Rigoulet, T. Nyström, Science 299, 1751-1753 (2003).
16. B. Liu et al., Cell 140, 257-267 (2010).
17. R. Spokoini et al., Cell Reports 2, 738-747 (2012).
18. M. A. Rujano et al., PLOS Biol. 4, e417 (2006).
19. M. R. Bufalino, B. DeVeale, D. van der Kooy, J. Cell Biol. 201, 523-530 (2013).
20. N. Erjavec, L. Larsson, J. Grantham, T. Nyström, Genes Dev. 21, 2410-2421 (2007).
21. P. Tessarz, M. Schwarz, A. Mogk, B. Bukau, Mol. Cell. Biol. 29, 3738-3745 (2009).
22. J. R. Glover, S. Lindquist, Cell 94, 73-82 (1998).
23. Materials and methods, figs. S1 to S3, and table S1 are available as supplementary materials on Science Online.
24. B. Liu et al., Cell 147, 959-961 (2011).
25. A. H. Tong et al., Science 294, 2364-2368 (2001).
26. A. H. Wong, C. Yan, Y. Shi, J. Biol. Chem. 287, 29251-29259 (2012).
27. D. Kaganovich, R. Kopito, J. Frydman, Nature 454, 1088-1095 (2008).
28. M. K. Sung, W. K. Huh, Yeast 24, 767-775 (2007).
29. R. Gupta et al., Nat. Methods 8, 879-884 (2011).
30. F. Eisele, D. H. Wolf, FEBS Lett. 582, 4143-4146 (2008).
31. D. Öling, F. Eisele, K. Kvint, T. Nyström, EMBO J. 33, 747 -761 (2014).
32. U. Kruegel et al., PLOS Genet. 7, e1002253 (2011).
33. D. Carmona-Gutierrez, K. U. Fröhlich, G. Kroemer, F. Madeo, Cell Death Differ. 17, 377-378 (2010).