830
Views
5
CrossRef citations to date
0
Altmetric
Perspective

Amyloid cannot resist identification

, &
Pages 464-468 | Received 04 Nov 2013, Accepted 12 Dec 2013, Published online: 23 Dec 2013

References

  • Greenwald J, Riek R. Biology of amyloid: structure, function, and regulation. Structure 2010; 18:1244 - 60; http://dx.doi.org/10.1016/j.str.2010.08.009; PMID: 20947013
  • Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D. Structure of the cross-beta spine of amyloid-like fibrils. Nature 2005; 435:773 - 8; http://dx.doi.org/10.1038/nature03680; PMID: 15944695
  • Saibil HR, Seybert A, Habermann A, Winkler J, Eltsov M, Perkovic M, Castaño-Diez D, Scheffer MP, Haselmann U, Chlanda P, et al. Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures. Proc Natl Acad Sci U S A 2012; 109:14906 - 11; http://dx.doi.org/10.1073/pnas.1211976109; PMID: 22927413
  • Shewmaker F, McGlinchey RP, Wickner RB. Structural insights into functional and pathological amyloid. J Biol Chem 2011; 286:16533 - 40; http://dx.doi.org/10.1074/jbc.R111.227108; PMID: 21454545
  • Wang X, Chapman MR. Curli provide the template for understanding controlled amyloid propagation. Prion 2008; 2:57 - 60; http://dx.doi.org/10.4161/pri.2.2.6746; PMID: 19098444
  • Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006; 75:333 - 66; http://dx.doi.org/10.1146/annurev.biochem.75.101304.123901; PMID: 16756495
  • Sarell CJ, Stockley PG, Radford SE. Assessing the causes and consequences of co-polymerization in amyloid formation. Prion 2013; 7:7; http://dx.doi.org/10.4161/pri.26415; PMID: 24025483
  • Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, Liebman SW. Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci U S A 2004; 101:12934 - 9; http://dx.doi.org/10.1073/pnas.0404968101; PMID: 15326312
  • Ross ED, Maclea KS, Anderson C, Ben-Hur A. A bioinformatics method for identifying Q/N-rich prion-like domains in proteins. Methods Mol Biol 2013; 1017:219 - 28; http://dx.doi.org/10.1007/978-1-62703-438-8_16; PMID: 23719919
  • Kryndushkin D, Pripuzova N, Burnett BG, Shewmaker F. Non-targeted identification of prions and amyloid-forming proteins from yeast and mammalian cells. J Biol Chem 2013; 288:27100 - 11; http://dx.doi.org/10.1074/jbc.M113.485359; PMID: 23926098
  • Liebman SW, Chernoff YO. Prions in yeast. Genetics 2012; 191:1041 - 72; http://dx.doi.org/10.1534/genetics.111.137760; PMID: 22879407
  • McGlinchey RP, Kryndushkin D, Wickner RB. Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci U S A 2011; 108:5337 - 41; http://dx.doi.org/10.1073/pnas.1102762108; PMID: 21402947
  • Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 1996; 15:3127 - 34; PMID: 8670813
  • Balbirnie M, Grothe R, Eisenberg DS. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc Natl Acad Sci U S A 2001; 98:2375 - 80; http://dx.doi.org/10.1073/pnas.041617698; PMID: 11226247
  • Li LB, Xu K, Bonini NM. Suppression of polyglutamine toxicity by the yeast Sup35 prion domain in Drosophila. J Biol Chem 2007; 282:37694 - 701; http://dx.doi.org/10.1074/jbc.M705211200; PMID: 17956866
  • Kryndushkin DS, Alexandrov IM, Ter-Avanesyan MD, Kushnirov VV. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 2003; 278:49636 - 43; http://dx.doi.org/10.1074/jbc.M307996200; PMID: 14507919
  • Saupe SJ. A short history of small s: a prion of the fungus Podospora anserina. Prion 2007; 1:110 - 5; http://dx.doi.org/10.4161/pri.1.2.4666; PMID: 19164916
  • Turcotte C, Roux A, Beauregard PB, Guérin R, Sénéchal P, Hajjar F, Rokeach LA. The calnexin-independent state does not compensate for all calnexin functions in Schizosaccharomyces pombe. FEMS Yeast Res 2007; 7:196 - 208; http://dx.doi.org/10.1111/j.1567-1364.2006.00145.x; PMID: 17328741
  • Silar P, Haedens V, Rossignol M, Lalucque H. Propagation of a novel cytoplasmic, infectious and deleterious determinant is controlled by translational accuracy in Podospora anserina. Genetics 1999; 151:87 - 95; PMID: 9872950
  • Wickner RB, Kryndushkin D, Shewmaker F, McGlinchey R, Edskes HK. Study of amyloids using yeast. Methods Mol Biol 2012; 849:321 - 46; http://dx.doi.org/10.1007/978-1-61779-551-0_22; PMID: 22528100
  • Halfmann R, Jarosz DF, Jones SK, Chang A, Lancaster AK, Lindquist S. Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 2012; 482:363 - 8; http://dx.doi.org/10.1038/nature10875; PMID: 22337056
  • Walther TC, Brickner JH, Aguilar PS, Bernales S, Pantoja C, Walter P. Eisosomes mark static sites of endocytosis. Nature 2006; 439:998 - 1003; http://dx.doi.org/10.1038/nature04472; PMID: 16496001
  • Deng C, Xiong X, Krutchinsky AN. Unifying fluorescence microscopy and mass spectrometry for studying protein complexes in cells. Mol Cell Proteomics 2009; 8:1413 - 23; http://dx.doi.org/10.1074/mcp.M800397-MCP200; PMID: 19269952
  • Kelly AC, Wickner RB. Saccharomyces cerevisiae: a sexy yeast with a prion problem. Prion 2013; 7:215 - 20; http://dx.doi.org/10.4161/pri.24845; PMID: 23764836
  • Tyedmers J, Madariaga ML, Lindquist S. Prion switching in response to environmental stress. PLoS Biol 2008; 6:e294; http://dx.doi.org/10.1371/journal.pbio.0060294; PMID: 19067491
  • Halfmann R, Lindquist S. Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits. Science 2010; 330:629 - 32; http://dx.doi.org/10.1126/science.1191081; PMID: 21030648
  • Allen KD, Wegrzyn RD, Chernova TA, Müller S, Newnam GP, Winslett PA, Wittich KB, Wilkinson KD, Chernoff YO. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. [PSI+] Genetics 2005; 169:1227 - 42; http://dx.doi.org/10.1534/genetics.104.037168; PMID: 15545639
  • Kelly AC, Shewmaker FP, Kryndushkin D, Wickner RB. Sex, prions, and plasmids in yeast. Proceedings of the National Academy of Sciences of the United States of America 2012.
  • Shewmaker F, Wickner RB, Tycko R. Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc Natl Acad Sci U S A 2006; 103:19754 - 9; http://dx.doi.org/10.1073/pnas.0609638103; PMID: 17170131
  • Bagriantsev SN, Gracheva EO, Richmond JE, Liebman SW. Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. Mol Biol Cell 2008; 19:2433 - 43; http://dx.doi.org/10.1091/mbc.E08-01-0078; PMID: 18353968
  • Lopez N, Aron R, Craig EA. Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+]. [RNQ+] Mol Biol Cell 2003; 14:1172 - 81; http://dx.doi.org/10.1091/mbc.E02-09-0593; PMID: 12631732
  • Ratovitski T, Chighladze E, Arbez N, Boronina T, Herbrich S, Cole RN, Ross CA. Huntingtin protein interactions altered by polyglutamine expansion as determined by quantitative proteomic analysis. Cell Cycle 2012; 11:2006 - 21; http://dx.doi.org/10.4161/cc.20423; PMID: 22580459
  • Xu G, Stevens SM Jr., Moore BD, McClung S, Borchelt DR. Cytosolic proteins lose solubility as amyloid deposits in a transgenic mouse model of Alzheimer-type amyloidosis. Hum Mol Genet 2013; 22:2765 - 74; http://dx.doi.org/10.1093/hmg/ddt121; PMID: 23512986
  • Gunawardena S, Her LS, Brusch RG, Laymon RA, Niesman IR, Gordesky-Gold B, Sintasath L, Bonini NM, Goldstein LS. Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila. Neuron 2003; 40:25 - 40; http://dx.doi.org/10.1016/S0896-6273(03)00594-4; PMID: 14527431
  • Nucifora FC Jr., Ellerby LM, Wellington CL, Wood JD, Herring WJ, Sawa A, Hayden MR, Dawson VL, Dawson TM, Ross CA. Nuclear localization of a non-caspase truncation product of atrophin-1, with an expanded polyglutamine repeat, increases cellular toxicity. J Biol Chem 2003; 278:13047 - 55; http://dx.doi.org/10.1074/jbc.M211224200; PMID: 12464607

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.