메뉴 건너뛰기




Volumn 27, Issue 20, 2008, Pages 2725-2735

Curing of the [URE3] prion by Btn2p, a Batten disease-related protein

Author keywords

Amyloid; Hook homologue; Ypr158p

Indexed keywords

GREEN FLUORESCENT PROTEIN; PRION PROTEIN; PROTEIN BTN2P; PROTEIN URE3; UNCLASSIFIED DRUG;

EID: 54349128824     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2008.198     Document Type: Article
Times cited : (91)

References (52)
  • 1
  • 3
    • 36048969163 scopus 로고    scopus 로고
    • Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance
    • Baxa U, Wickner RB, Steven AC, Anderson D, Marekov L, Yau W-M, Tycko R (2007) Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance. Biochemistry 46: 13149-13162
    • (2007) Biochemistry , vol.46 , pp. 13149-13162
    • Baxa, U.1    Wickner, R.B.2    Steven, A.C.3    Anderson, D.4    Marekov, L.5    Yau, W.-M.6    Tycko, R.7
  • 4
    • 27144451227 scopus 로고    scopus 로고
    • Prion generation in vitro: Amyloid of Ure2p is infectious
    • Brachmann A, Baxa U, Wickner RB (2005) Prion generation in vitro: amyloid of Ure2p is infectious. EMBO J 24: 3082-3092
    • (2005) EMBO J , vol.24 , pp. 3082-3092
    • Brachmann, A.1    Baxa, U.2    Wickner, R.B.3
  • 7
    • 0033764930 scopus 로고    scopus 로고
    • The yeast model for Batten disease: Mutations in BTN1, BTN2, andHSP30 alter pH homeostasis
    • Chattopadhyay S, Muzaffar NE, Sherman F, Pearce DA (2000) The yeast model for Batten disease: mutations in BTN1, BTN2, andHSP30 alter pH homeostasis. J Bacteriol 182: 6418-6423
    • (2000) J Bacteriol , vol.182 , pp. 6418-6423
    • Chattopadhyay, S.1    Muzaffar, N.E.2    Sherman, F.3    Pearce, D.A.4
  • 8
    • 0036689845 scopus 로고    scopus 로고
    • Interaction with Btn2p is required for localization of Rsg1p: Btn2p-mediated changes in arginine uptake in Saccharomyces cerevisiae
    • Chattopadhyay S, Pearce DA (2002) Interaction with Btn2p is required for localization of Rsg1p: Btn2p-mediated changes in arginine uptake in Saccharomyces cerevisiae. Eukaryot Cell 1: 606-612
    • (2002) Eukaryot Cell , vol.1 , pp. 606-612
    • Chattopadhyay, S.1    Pearce, D.A.2
  • 12
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: The story of [PIN]
    • Derkatch IL, Bradley ME, Hong JY, Liebman SW (2001) Prions affect the appearance of other prions: the story of [PIN]. Cell 106: 171-182
    • (2001) Cell , vol.106 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 14
    • 0033574042 scopus 로고    scopus 로고
    • The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments
    • Edskes HK, Gray VT, Wickner RB (1999) The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc Natl Acad Sci USA 96: 1498-1503
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1498-1503
    • Edskes, H.K.1    Gray, V.T.2    Wickner, R.B.3
  • 18
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover JR, Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 19
    • 0031771756 scopus 로고    scopus 로고
    • Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA
    • Hellmuth K, Lau DM, Bischoff FR, Kunzler M, Hurt E, Simos G (1998) Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA. Mol Cell Biol 18: 6374-6386
    • (1998) Mol Cell Biol , vol.18 , pp. 6374-6386
    • Hellmuth, K.1    Lau, D.M.2    Bischoff, F.R.3    Kunzler, M.4    Hurt, E.5    Simos, G.6
  • 21
    • 1942518319 scopus 로고    scopus 로고
    • Propagation of yeast [PSI+] prion impaired by factors that regulate Hsp70 substrate binding
    • Jones G, Song Y, Chung S, Masison DC (2004) Propagation of yeast [PSI+] prion impaired by factors that regulate Hsp70 substrate binding. Mol Cell Biol 24: 3928-3937
    • (2004) Mol Cell Biol , vol.24 , pp. 3928-3937
    • Jones, G.1    Song, Y.2    Chung, S.3    Masison, D.C.4
  • 23
    • 33846130921 scopus 로고    scopus 로고
    • Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast
    • Kama R, Robinson M, Gerst JE (2007) Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast. Mol Cell Biol 27: 605-621
    • (2007) Mol Cell Biol , vol.27 , pp. 605-621
    • Kama, R.1    Robinson, M.2    Gerst, J.E.3
  • 24
    • 13844311439 scopus 로고    scopus 로고
    • Interaction among Btn1p, Btn2p, and Ist2p reveals potential interplay among the vacuole, amino acid levels, and ion homeostasis in the yeast Saccharomyces cerevisiae
    • Kim Y, Chattopadhyay S, Locke S, Pearce DA (2005) Interaction among Btn1p, Btn2p, and Ist2p reveals potential interplay among the vacuole, amino acid levels, and ion homeostasis in the yeast Saccharomyces cerevisiae. Eukaryot Cell 4: 281-288
    • (2005) Eukaryot Cell , vol.4 , pp. 281-288
    • Kim, Y.1    Chattopadhyay, S.2    Locke, S.3    Pearce, D.A.4
  • 25
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • King CY, Diaz-Avalos R (2004) Protein-only transmission of three yeast prion strains. Nature 428: 319-323
    • (2004) Nature , vol.428 , pp. 319-323
    • King, C.Y.1    Diaz-Avalos, R.2
  • 26
    • 0037189549 scopus 로고    scopus 로고
    • Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions
    • Kryndushkin D, Smirnov VN, Ter-Avanesyan MD, Kushnirov VV (2002) Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277: 23702-23708
    • (2002) J Biol Chem , vol.277 , pp. 23702-23708
    • Kryndushkin, D.1    Smirnov, V.N.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 27
    • 34250311267 scopus 로고    scopus 로고
    • Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae
    • Kryndushkin D, Wickner RB (2007) Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae. Mol Biol Cell 18: 2149-2154
    • (2007) Mol Biol Cell , vol.18 , pp. 2149-2154
    • Kryndushkin, D.1    Wickner, R.B.2
  • 29
    • 0032503963 scopus 로고    scopus 로고
    • Structure and replication of yeast prions
    • Kushnirov VV, Ter-Avanesyan MD (1998) Structure and replication of yeast prions. Cell 94: 13-16
    • (1998) Cell , vol.94 , pp. 13-16
    • Kushnirov, V.V.1    Ter-Avanesyan, M.D.2
  • 32
    • 9744254471 scopus 로고    scopus 로고
    • Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway
    • Luiro K, Yliannala K, Ahtiainen L, Maunu H, Jarvela I, Kyttala A, Jalanko A (2004) Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway. Hum Mol Genet 13: 3017-3027
    • (2004) Hum Mol Genet , vol.13 , pp. 3017-3027
    • Luiro, K.1    Yliannala, K.2    Ahtiainen, L.3    Maunu, H.4    Jarvela, I.5    Kyttala, A.6    Jalanko, A.7
  • 34
    • 0037053566 scopus 로고    scopus 로고
    • Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • Meriin AB, Zhang X, He X, Newnam GP, Chernoff YO, Sherman MY (2002) Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J Cell Biol 157: 997-1004
    • (2002) J Cell Biol , vol.157 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3    Newnam, G.P.4    Chernoff, Y.O.5    Sherman, M.Y.6
  • 35
    • 0034462603 scopus 로고    scopus 로고
    • URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • Moriyama H, Edskes HK, Wickner RB (2000) [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol Cell Biol 20: 8916-8922
    • (2000) Mol Cell Biol , vol.20 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 36
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO (1999) Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol Cell Biol 19: 1325-1333
    • (1999) Mol Cell Biol , vol.19 , pp. 1325-1333
    • Newnam, G.P.1    Wegrzyn, R.D.2    Lindquist, S.L.3    Chernoff, Y.O.4
  • 37
    • 0032905252 scopus 로고    scopus 로고
    • Action of BTN1, the yeast ortholog of the gene mutated in Batten disease
    • Pearce DA, Ferea T, Nosel SA, Das B, Sherman F (1999) Action of BTN1, the yeast ortholog of the gene mutated in Batten disease. Nat Genet 22: 55-58
    • (1999) Nat Genet , vol.22 , pp. 55-58
    • Pearce, D.A.1    Ferea, T.2    Nosel, S.A.3    Das, B.4    Sherman, F.5
  • 38
    • 1242296312 scopus 로고    scopus 로고
    • URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast
    • Roberts BT, Moriyama H, Wickner RB (2004) [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast 21: 107-117
    • (2004) Yeast , vol.21 , pp. 107-117
    • Roberts, B.T.1    Moriyama, H.2    Wickner, R.B.3
  • 39
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443: 780-786
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 40
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Guthrie C, Fink GR eds, San Diego: Academic Press
    • Sherman F (1991) Getting started with yeast. In Guide to Yeast Genetics and Molecular Biology Guthrie C, Fink GR (eds), Vol. 194, pp 3-21. San Diego: Academic Press
    • (1991) Guide to Yeast Genetics and Molecular Biology , vol.194 , pp. 3-21
    • Sherman, F.1
  • 41
    • 33845938549 scopus 로고    scopus 로고
    • Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure
    • Shewmaker F, Wickner RB, Tycko R (2006) Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure. Proc Natl Acad Sci USA 103: 19754-19759
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 19754-19759
    • Shewmaker, F.1    Wickner, R.B.2    Tycko, R.3
  • 42
    • 3142677196 scopus 로고    scopus 로고
    • Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway
    • Shintani T, Klionsky DJ (2004) Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway. J Biol Chem 279: 29889-29894
    • (2004) J Biol Chem , vol.279 , pp. 29889-29894
    • Shintani, T.1    Klionsky, D.J.2
  • 43
    • 33745586752 scopus 로고    scopus 로고
    • Expression of an expanded polyglutamine domain in yeast causes death with apoptotic markers
    • Sokolov S, Pozniakowsky A, Bocharova N, Knorre D, Severin F (2006) Expression of an expanded polyglutamine domain in yeast causes death with apoptotic markers. Biochim Biophys Acta 1757: 660-666
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 660-666
    • Sokolov, S.1    Pozniakowsky, A.2    Bocharova, N.3    Knorre, D.4    Severin, F.5
  • 44
    • 0032961825 scopus 로고    scopus 로고
    • Genetic dissection of endocytic trafficking in Drosophila using a horseradish peroxidase-bride of sevenless chimera: Hook is required for normal maturation of multivesicular endosomes
    • Sunio A, Metcalf AB, Kramer H (1999) Genetic dissection of endocytic trafficking in Drosophila using a horseradish peroxidase-bride of sevenless chimera: hook is required for normal maturation of multivesicular endosomes. Mol Biol Cell 10: 847-859
    • (1999) Mol Biol Cell , vol.10 , pp. 847-859
    • Sunio, A.1    Metcalf, A.B.2    Kramer, H.3
  • 46
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M, Chien P, Naber N, Cooke R, Weissman JS (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428: 323-328
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 47
    • 0035809910 scopus 로고    scopus 로고
    • The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins
    • Walenta JH, Didier AJ, Liu X, Kramer H (2001) The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins. J Cell Biol 152: 923-934
    • (2001) J Cell Biol , vol.152 , pp. 923-934
    • Walenta, J.H.1    Didier, A.J.2    Liu, X.3    Kramer, H.4
  • 48
    • 17044376248 scopus 로고    scopus 로고
    • Elevation of Hook1 in a disease model of Batten disease does not affect a novel interaction between Ankyrin G and Hook1
    • Weimer JM, Chattopadhyay S, Custer AW, Pearce DA (2005) Elevation of Hook1 in a disease model of Batten disease does not affect a novel interaction between Ankyrin G and Hook1. Biochem Biophys Res Commun 330: 1176-1181
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 1176-1181
    • Weimer, J.M.1    Chattopadhyay, S.2    Custer, A.W.3    Pearce, D.A.4
  • 49
    • 0028308104 scopus 로고
    • URE3] as an altered URE2 protein: Evidence for a prion analog in S. cerevisiae
    • Wickner RB (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in S. cerevisiae. Science 264: 566-569
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 52
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy molecular machinery for self-eating
    • Yorimitsu T, Klionsky DJ (2005) Autophagy molecular machinery for self-eating. Cell Death Differ 12: 1542-1552
    • (2005) Cell Death Differ , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.