Unraveling the mechanism of cell death induced by chemical fibrils

Nature Chemical Biology

Volumn 10, Issue 11, 2014, Pages 969-976

  Julien, Olivier ^a   Kampmann, Martin ^a,b   Bassik, Michael C ^b,e   Zorn, Julie A ^a,f   Venditto, Vincent J ^b   Shimbo, Kazutaka ^a,g   Agard, Nicholas J ^a,h   Shimada, Kenichi ^c   Rheingold, Arnold L ^d   Stockwell, Brent R ^c   Weissman, Jonathan S ^a,b   Wells, James A ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c Och Spine at New York Presbyterian Hospitals   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^f UNIVERSITY OF CALIFORNIA   (United States)

^g AJINOMOTO CO INC   (Japan)

^h Department of Chemistry University of California San Diego ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1541; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ANTINEOPLASTIC AGENT; CELL DNA; LIPOSOME; POLYSORBATE 80; PROCASPASE 3; RAB PROTEIN; RAB1A PROTEIN; RAB2A PROTEIN; RAB39A PROTEIN; RAB7A PROTEIN; RABEP1 PROTEIN; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG; BENZAMIDE DERIVATIVE; CASPASE 3; COUMARIN DERIVATIVE;

ACIDIFICATION; ACTIN POLYMERIZATION; ANTINEOPLASTIC ACTIVITY; APOPTOSIS; ARTICLE; CELL CULTURE; CELL DEATH; CELL MIGRATION; CELLULAR DISTRIBUTION; CHEMICAL STRUCTURE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOTOXICITY; DRUG MECHANISM; DRUG STRUCTURE; DRUG SYNTHESIS; DRUG UPTAKE; EC50; EMBRYO; ENDOCYTOSIS; ENZYME ACTIVATION; ENZYME INHIBITION; GENE SILENCING; GENETIC CODE; HUMAN; HUMAN CELL; HYDROGEN BOND; IN VITRO STUDY; K562 CELL LINE; LIGHT SCATTERING; LYSOSOME; MOLECULAR SIZE; MOLECULAR WEIGHT; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN EXPRESSION; RNA ANALYSIS; SIGNAL TRANSDUCTION; AMINO ACID SEQUENCE; BIOLOGICAL MODEL; CELL PROLIFERATION; CHEMISTRY; DOSE RESPONSE; DRUG EFFECTS; METABOLISM; STRUCTURE ACTIVITY RELATION; TUMOR CELL CULTURE;

AMINO ACID SEQUENCE; BENZAMIDES; CASPASE 3; CELL DEATH; CELL PROLIFERATION; COUMARINS; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; K562 CELLS; LYSOSOMES; MODELS, BIOLOGICAL; MOLECULAR STRUCTURE; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR CELLS, CULTURED;

EID: 84919798910     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1639     Document Type: Article

References (33)

1. Jucker, M. & Walker, L.C. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501, 45-51 (2013).
2. Eisenberg, D. & Jucker, M. The amyloid state of proteins in human diseases. Cell 148, 1188-1203 (2012).
3. Wolan, D.W., Zorn, J.A., Gray, D.C. & Wells, J.A. Small-molecule activators of a proenzyme. Science 326, 853-858 (2009).
4. Zorn, J.A., Wille, H., Wolan, D.W. & Wells, J.A. Self-assembling small molecules form nanofibrils that bind procaspase-3 to promote activation. J. Am. Chem. Soc. 133, 19630-19633 (2011).
5. Zorn, J.A., Wolan, D.W., Agard, N.J. & Wells, J.A. Fibrils colocalize caspase-3 with procaspase-3 to foster maturation. J. Biol. Chem. 287, 33781-33795 (2012).
6. Bassik, M.C. et al. Rapid creation and quantitative monitoring of high coverage shRNA libraries. Nat. Methods 6, 443-445 (2009).
7. Bassik, M.C. et al. A systematic Mammalian genetic interaction map reveals pathways underlying ricin susceptibility. Cell 152, 909-922 (2013).
8. Kampmann, M., Bassik, M.C. & Weissman, J.S. Integrated platform for genome-wide screening and construction of high-density genetic interaction maps in mammalian cells. Proc. Natl. Acad. Sci. USA 110, E2317-E2326 (2013).
9. Weiss, W.A., Taylor, S.S. & Shokat, K.M. Recognizing and exploiting differences between RNAi and small-molecule inhibitors. Nat. Chem. Biol. 3, 739-744 (2007).
10. Crawford, E.D. et al. The DegraBase: a database of proteolysis in healthy and apoptotic human cells. Mol. Cell. Proteomics 12, 813-824 (2013).
11. Mahrus, S. et al. Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini. Cell 134, 866-876 (2008).
12. Wiita, A.P., Seaman, J.E. & Wells, J.A. Global analysis of cellular proteolysis by selective enzymatic labeling of protein N-termini. Methods Enzymol. 544, 327-358 (2014).
13. Wolpaw, A.J. et al. Modulatory profiling identifies mechanisms of small molecule-induced cell death. Proc. Natl. Acad. Sci. USA 108, E771-E780 (2011).
14. Holmes, B.B. et al. Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc. Natl. Acad. Sci. USA 110, E3138-E3147 (2013).
15. Owen, S.C., Doak, A.K., Wassam, P., Shoichet, M.S. & Shoichet, B.K. Colloidal aggregation affects the efficacy of anticancer drugs in cell culture. ACS Chem. Biol. 7, 1429-1435 (2012).
16. Owen, S.C. et al. Colloidal drug formulations can explain "bell-shaped" concentration-response curves. ACS Chem. Biol. 9, 777-784 (2014).
17. Kampmann, M., Bassik, M.C. & Weissman, J.S. Functional genomics platform for pooled screening and generation of mammalian genetic interaction maps. Nat. Protoc. 9, 1825-1847 (2014).
18. Tisdale, E.J., Bourne, J.R., Khosravi-Far, R., Der, C.J. & Balch, W.E. GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. J. Cell Biol. 119, 749-761 (1992).
19. Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J. & van Deurs, B. Rab7: a key to lysosome biogenesis. Mol. Biol. Cell 11, 467-480 (2000).
20. Stenmark, H., Vitale, G., Ullrich, O. & Zerial, M. Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell 83, 423-432 (1995).
21. Seto, S., Tsujimura, K. & Koide, Y. Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes. Traffic 12, 407-420 (2011).
22. Stenmark, H. Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol. 10, 513-525 (2009).
23. Münch, C., O'Brien, J. & Bertolotti, A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. USA 108, 3548-3553 (2011).
24. Weinstein, J.N., Yoshikami, S., Henkart, P., Blumenthal, R. & Hagins, W.A. Liposome-cell interaction: transfer and intracellular release of a trapped fluorescent marker. Science 195, 489-492 (1977).
25. Shimbo, K. et al. Quantitative profiling of caspase-cleaved substrates reveals different drug-induced and cell-type patterns in apoptosis. Proc. Natl. Acad. Sci. USA 109, 12432-12437 (2012).
26. Wiita, A.P. et al. Global cellular response to chemotherapy-induced apoptosis. Elife 2, e01236 (2013).
27. Fraley, C. & Raftery, A.E. Model-based clustering, discriminant analysis, and density estimation. J. Am. Stat. Assoc. 97, 611-631 (2002).
28. Duewell, P. et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature 464, 1357-1361 (2010).
29. Halle, A. et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-β. Nat. Immunol. 9, 857-865 (2008).
30. Huff, M.E., Balch, W.E. & Kelly, J.W. Pathological and functional amyloid formation orchestrated by the secretory pathway. Curr. Opin. Struct. Biol. 13, 674-682 (2003).
31. Novitskaya, V., Bocharova, O.V., Bronstein, I. & Baskakov, I.V. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J. Biol. Chem. 281, 13828-13836 (2006).
32. Yao, J. et al. Neuroprotection by cyclodextrin in cell and mouse models of Alzheimer disease. J. Exp. Med. 209, 2501-2513 (2012).
33. Walsh, D.M. & Selkoe, D.J. Aβ oligomers - a decade of discovery. J. Neurochem. 101, 1172-1184 (2007).