712
Views
2
CrossRef citations to date
0
Altmetric
Extra Views

Spatial sequestration and oligomer remodeling during de novo [PSI+] formation

&
Pages 332-337 | Received 23 Jun 2017, Accepted 13 Aug 2017, Published online: 12 Oct 2017

REFERENCES

  • Diaz-Espinoza R, Soto C. Generation of prions in vitro and the protein-only hypothesis. Prion. 2010;4(2):53–9. doi:10.4161/pri.4.2.11960. PMID:20448454.
  • Liebman SW, Chernoff YO. Prions in yeast. Genetics. 2012;191(4):1041–72. doi:10.1534/genetics.111.137760. PMID:22879407.
  • Aigle M, Lacroute F. Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast. Mol Gen Genet. 1975;136(4):327–35. doi:10.1007/BF00341717. PMID:16095000.
  • Lancaster AK, Bardill JP, True HL, Masel J. The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system. Genetics. 2010;184(2):393–400. doi:10.1534/genetics.109.110213. PMID:19917766.
  • Lund PM, Cox BS. Reversion analysis of [psi-] mutations in Saccharomyces cerevisiae. Genet Res. 1981;37(2):173–82. doi:10.1017/S0016672300020140. PMID:7021322.
  • King CY, Diaz-Avalos R. Protein-only transmission of three yeast prion strains. Nature. 2004;428(6980):319–23. doi:10.1038/nature02391. PMID:15029195.
  • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. Conformational variations in an infectious protein determine prion strain differences. Nature. 2004;428(6980):323–8. doi:10.1038/nature02392. PMID:15029196.
  • Chernoff YO, Derkach IL, Inge-Vechtomov SG. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr Genet. 1993;24(3):268–70. doi:10.1007/BF00351802. PMID:8221937.
  • Derkatch IL, Bradley ME, Hong JY, Liebman SW. Prions affect the appearance of other prions: The story of [PIN(+)]. Cell. 2001;106(2):171–82. S0092-8674(01)00427-5 [pii] doi:10.1016/S0092-8674(01)00427-5. PMID:11511345.
  • Osherovich LZ, Weissman JS. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell. 2001;106(2):183–94. doi:10.1016/S0092-8674(01)00440-8. PMID:11511346.
  • Sondheimer N, Lindquist S. Rnq1: An epigenetic modifier of protein function in yeast. Mol Cell. 2000;5(1):163–72. doi:10.1016/S1097-2765(00)80412-8. PMID:10678178.
  • Zhou P, Derkatch IL, Liebman SW. The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)]. Mol Microbiol. 2001;39(1):37–46. mmi2224 [pii] doi:10.1046/j.1365-2958.2001.02224.x. PMID:11123686.
  • Ganusova EE, Ozolins LN, Bhagat S, Newnam GP, Wegrzyn RD, Sherman MY, Chernoff YO. Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Mol Cell Biol. 2006;26(2):617–29. doi:10.1128/MCB.26.2.617-629.2006. PMID:16382152.
  • Sharma J, Wisniewski BT, Paulson E, Obaoye JO, Merrill SJ, Manogaran AL. De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers. Sci Rep. 2017;7(1):76. doi:10.1038/s41598-017-00135-6. PMID:28250435.
  • Higuchi-Sanabria R, Pernice WM, Vevea JD, Alessi Wolken DM, Boldogh IR, Pon LA. Role of asymmetric cell division in lifespan control in Saccharomyces cerevisiae. FEMS Yeast Res. 2014;14(8):1133–46. doi:10.1111/1567-1364.12216. PMID:25263578.
  • Erjavec N, Larsson L, Grantham J, Nyström T. Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p. Genes Dev. 2007;21(19):2410–21. doi:10.1101/gad.439307. PMID:17908928.
  • Song J, Yang Q, Yang J, Larsson L, Hao X, Zhu X, Malmgren-Hill S, Cvijovic M, Fernandez-Rodriguez J, Grantham J, et al. Essential genetic interactors of SIR2 required for spatial sequestration and asymmetrical inheritance of protein aggregates. PLoS Genet. 2014;10(7):e1004539. doi:10.1371/journal.pgen.1004539. PMID:25079602.
  • Kumar R, Nawroth PP, Tyedmers J. Prion aggregates are recruited to the insoluble protein deposit (IPOD) via myosin 2-based vesicular transport. PLoS Genet. 2016;12(9):e1006324. doi:10.1371/journal.pgen.1006324. PMID:27689885.
  • Saarikangas J, Barral Y. Protein aggregates are associated with replicative aging without compromising protein quality control. Elife. 2015;4:e06197. doi:10.7554/eLife.06197. PMID:26544680.
  • Saarikangas J, Caudron F, Prasad R, Moreno DF, Bolognesi A, Aldea M, Barral Y. Compartmentalization of ER-bound chaperone confines protein deposit formation to the aging yeast cell. Curr Biol. 2017;27(6):773–783. doi:10.1016/j.cub.2017.01.069. PMID:28262489.
  • 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(49):49636–43. doi:10.1074/jbc.M307996200. PMID:14507919.