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Protein misfolding in Dictyostelium: Using a freak of nature to gain insight into a universal problem

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Pages 339-346 | Received 31 Aug 2015, Accepted 18 Sep 2015, Published online: 21 Dec 2015

REFERENCES

  • Tanaka EM, Reddien PW. The cellular basis for animal regeneration. Dev Cell 2011; 21:172-85; PMID:21763617; http://dx.doi.org/10.1016/j.devcel.2011.06.016
  • Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 2005; 6:435-50; PMID:15931169; http://dx.doi.org/10.1038/nrg1616
  • Sugiyama S, Tanaka M. Self-propagating amyloid as a critical regulator for diverse cellular functions. J Biochem 2014; 155:345-51; PMID:24711463; http://dx.doi.org/10.1093/jb/mvu026
  • 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; PMID:22337056; http://dx.doi.org/10.1038/nature10875
  • Gitler AD, Shorter J. RNA-binding proteins with prion-like domains in ALS and FTLD-U. Prion 2011; 5:179-87; PMID:21847013; http://dx.doi.org/10.4161/pri.5.3.17230
  • Maniecka Z, Polymenidou M. From nucleation to widespread propagation: A prion-like concept for ALS. Virus Res 2015; 207:94-105; PMID:25656065; http://dx.doi.org/10.1016/j.virusres.2014.12.032
  • Kim HJ, Kim NC, Wang YD, Scarborough EA, Moore J, et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013; 495:467-73; PMID:23455423; http://dx.doi.org/10.1038/nature11922
  • Nomura T, Watanabe S, Kaneko K, Yamanaka K, Nukina N, Furukawa Y. Intranuclear Aggregation of Mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis. J Biol Chem 2014; 289:1192-202; PMID:24280224; http://dx.doi.org/10.1074/jbc.M113.516492
  • Patel A, Lee HO, Jawerth L, Maharana S, Jahnel M, Hein MY, Stoynov S, Mahamid J, Saha S, Franzmann TM, et al. A Liquid-to-Solid Phase transition of the ALS protein FUS accelerated by disease mutation. Cell 2015; 162:1066-1077; PMID:26317470; http://dx.doi.org/10.1016/j.cell.2015.07.047
  • Liebman SW, Chernoff YO. Prions in yeast. Genetics 2012; 191:1041-72; PMID:22879407; http://dx.doi.org/10.1534/genetics.111.137760
  • Wickner RB, Shewmaker FP, Bateman DA, Edskes HK, Gorkovskiy A, Dayani Y, Bezsonov EE. Yeast prions: structure, biology and prion-handling systems. Microbiol Mol Biol Rev 2015; 79:1-17; PMID:25631286; http://dx.doi.org/10.1128/MMBR.00041-14
  • Michelitsch MDM, Weissman JSJ. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci USA 2000; 97:11910-5; PMID:11050225; http://dx.doi.org/10.1073/pnas.97.22.11910
  • Malinovska L, Palm S, Gibson K, Verbavatz JM, Alberti S. Dictyostelium discoideumhas a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation. Proc Natl Acad Sci USA 2015; 112(20):E2620-9, 201504459-10
  • King OD, Gitler AD, Shorter J. The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res 2012; 1462:61-80; PMID:22445064; http://dx.doi.org/10.1016/j.brainres.2012.01.016
  • Malinovska L, Kroschwald S, Alberti S. Protein disorder, prion propensities, and self-organizing macromolecular collectives. Biochim Biophys Acta 2013; 1834:1-14; PMID:23451353; http://dx.doi.org/10.1016/j.bbapap.2012.08.018
  • Uversky VN. A decade and a half of protein intrinsic disorder: Biology still waits for physics. Protein Sci 2013; 22:693-724; PMID:23553817; http://dx.doi.org/10.1002/pro.2261
  • Gemayel R, Chavali S, Pougach K, Legendre M, Zhu B, Boeynaems S, van der Zande E, Gevaert K, Rousseau F, Schymkowitz J, et al. Variable Glutamine-Rich repeats modulate transcription factor activity. Mol Cell 2015; 59:615-27; PMID:26257283; http://dx.doi.org/10.1016/j.molcel.2015.07.003
  • Krobitsch S, Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci USA 2000; 97:1589-94; PMID:10677504; http://dx.doi.org/10.1073/pnas.97.4.1589
  • Brignull HR, Morley JF, Garcia SM, Morimoto RI. Modeling polyglutamine pathogenesis in C elegans Methods in Enzymology. Elsevier 2006; 412:256-82.
  • Jana NR, Tanaka M, Wang GH, Nukina N. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum Mol Genet 2000; 9:2009-18; PMID:10942430; http://dx.doi.org/10.1093/hmg/9.13.2009
  • Halfmann R, Alberti S, Krishnan R, Lyle N, Lyle N, O'Donnell CW, O'Donnell CW, King OD, Berger B, Berger B, et al. Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Mol Cell 2011; 43:72-84; PMID:21726811; http://dx.doi.org/10.1016/j.molcel.2011.05.013
  • Lu X, Murphy RM. Asparagine repeat peptides: aggregation kinetics and comparison with glutamine repeats. Biochemistry 2015; 54:4784-94; PMID:26204228; http://dx.doi.org/10.1021/acs.biochem.5b00644
  • Latonen L. Nucleolar aggresomes as counterparts of cytoplasmic aggresomes in proteotoxic stress. Bioessays 2011; 33:386-95; PMID:21425306; http://dx.doi.org/10.1002/bies.201100008
  • Park SH, Kukushkin Y, Gupta R, Chen T, Konagai A, Hipp MS, et al. PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the SIS1P chaperone. Cell 2013; 154:134-45; PMID:23791384; http://dx.doi.org/10.1016/j.cell.2013.06.003
  • Ortega Z. Ubiquitin-proteasome system involvement in Huntington's disease. Frontiers Mol Neuroscience 2014; 7:77; PMID:25324717; http://dx.doi.org/10.3389/fnmol.2014.00077
  • Aguilaniu H, Gustafsson L, Rigoulet M, Nystrom T. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 2003; 299:1751-3; PMID:12610228; http://dx.doi.org/10.1126/science.1080418
  • Rujano MA, Bosveld F, Salomons FA, Dijk F, van Waarde MAWH, et al. Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes. PLoS Biol 2006; 4:e417; PMID:17147470; http://dx.doi.org/10.1371/journal.pbio.0040417
  • Castillo DI, Queller DC, Strassmann JE. Cell condition, competition, and chimerism in the social amoeba Dictyostelium discoideum. Ethology Ecol Evolution 2011; 23:262-73; http://dx.doi.org/10.1080/03949370.2011.568526
  • Kroschwald S, Maharana S, Mateju D, Malinovska L, Nüske E, Poser I, Richter D, Alberti S. Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules. Elife 2015; 4:e06807; PMID:26238190; http://dx.doi.org/10.7554/eLife.06807