Conserved features of intermediates in amyloid assembly determine their benign or toxic states

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 28, 2012, Pages 11172-11177

  Krishnan, Rajaraman ^a,d   Goodman, Jessica L ^a   Mukhopadhyay, Samrat ^b,e   Pacheco, Chris D ^a,f   Lemke, Edward A ^b,g   Deniz, Ashok A ^b   Lindquist, Susan ^a,c  

^a WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^d NeuroPhage Pharmaceuticals   (United States)

^e INDIAN INSTITUTE OF SCIENCE EDUCATION AND RESEARCH MOHALI   (India)

^f HighRes Biosolutions   (United States)

^g EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

4,5 DIANILINOPHTHALIMIDE; AMPHOTERICIN B; CLOTRIMAZOLE; EPIGALLOCATECHIN GALLATE; FLUORESCENT DYE; FUNGAL PROTEIN; NAPHTHALIMIDE DERIVATIVE; OLIGOMER; PROTEIN ANTIBODY; SUP35 PROTEIN; UNCLASSIFIED DRUG;

ANISOTROPY; ARTICLE; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; MOLECULAR PROBE; MOLECULAR SIZE; NEUROBLASTOMA CELL; NEUROTOXICITY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN STRUCTURE;

ALZHEIMER DISEASE; AMYLOID; ANISOTROPY; CONSERVED SEQUENCE; DETERGENTS; FLUORESCENT DYES; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; NEURONS; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; TYROSINE;

EID: 84863973455     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1209527109     Document Type: Article

References (35)

1. Glabe CG (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283:29639-29643.
2. Walsh DM, et al. (1999) Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 274:25945-25952.
3. Harper JD, Lieber CM, Lansbury PT, Jr (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chem Biol 4:951-959. (Pubitemid 28050379)
4. Serio TR, et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289:1317-1321. (Pubitemid 30656041)
5. Shorter J, Lindquist S (2004) Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304:1793-1797. (Pubitemid 38787894)
6. Bemporad F, Chiti F (2012) Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem Biol 19:315-327.
7. Li S, et al. (2009) Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 62:788-801.
8. Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8:101-112. (Pubitemid 46432529)
9. Resenberger UK, et al. (2011) The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication. Embo J 30:2057-2070.
10. BucciantiniM, et al. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416:507-511. (Pubitemid 34288846)
11. Demuro A, et al. (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294-17300. (Pubitemid 41389198)
12. Campioni S, et al. (2010) A causative link between the structure of aberrant protein oligomers and their toxicity. Nat Chem Biol 6:140-147.
13. Bieschke J, et al. (2011) Small-molecule conversion of toxic oligomers to nontoxic beta-sheet-rich amyloid fibrils. Nat Chem Biol 8:93-101.
14. Shorter J, Lindquist S (2005) Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 6:435-450. (Pubitemid 40733889)
15. Halfmann R, et al. (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482:363-368.
16. Suzuki G, Shimazu N, Tanaka M (2012) A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress. Science 336:355-359.
17. Kayed R, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300:486-489. (Pubitemid 36444329)
18. Krishnan R, Lindquist SL (2005) Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435:765-772. (Pubitemid 40839721)
19. Mukhopadhyay S, Nayak PK, Udgaonkar JB, Krishnamoorthy G (2006) Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics. J Mol Biol 358:935-942. (Pubitemid 44382447)
20. Mukhopadhyay S, Deniz AA (2007) Fluorescence from diffusing single molecules illuminates biomolecular structure and dynamics. J Fluoresc 17:775-783. (Pubitemid 350075696)
21. Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S, Deniz AA (2007) A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci USA 104:2649-2654. (Pubitemid 46327934)
22. Marme N, Knemeyer JP, Sauer M, Wolfrum J (2003) Inter- and intramolecular fluorescence quenching of organic dyes by tryptophan. Bioconjug Chem 14:1133-1139. (Pubitemid 37449040)
23. Kayed R, et al. (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener 2:18.
24. Feng BY, et al. (2008) Small-molecule aggregates inhibit amyloid polymerization. Nat Chem Biol 4:197-199. (Pubitemid 351264126)
25. Ehrnhoefer DE, et al. (2008) EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol 15:558-566. (Pubitemid 351799141)
26. Xi YG, Ingrosso L, Ladogana A, Masullo C, Pocchiari M (1992) Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation. Nature 356:598-601.
27. Sackett DL, Wolff J (1987) Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces. Anal Biochem 167:228-234.
28. Dobson CM (1999) Protein misfolding, evolution and disease. Trends Biochem Sci 24:329-332.
29. Laganowsky A, et al. (2012) Atomic view of a toxic amyloid small oligomer. Science 335:1228-1231.
30. Bolognesi B, et al. (2010) ANS binding reveals common features of cytotoxic amyloid species. ACS Chem Biol 5:735-740.
31. Wang X, Smith DR, Jones JW, Chapman MR (2007) In vitro polymerization of a functional Escherichia coli amyloid protein. J Biol Chem 282:3713-3719. (Pubitemid 47084435)
32. Fowler DM, et al. (2006) Functional amyloid formation within mammalian tissue. PLoS Biol 4:e6.
33. Alberti S, Halfmann R, King O, Kapila A, Lindquist S (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137:146-158.
34. Halfmann R, et al. (2011) Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Mol Cell 43:72-84.
35. Treusch S, et al. (2011) Functional links between Abeta toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast. Science 334:1241-1245.