메뉴 건너뛰기




Volumn 7, Issue 12, 2012, Pages

Nuclear Import of UBL-Domain Protein Mdy2 Is Required for Heat-Induced Stress Response in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; PROTEIN MDY2; PROTEIN PAB1; UNCLASSIFIED DRUG;

EID: 84871675341     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0052956     Document Type: Article
Times cited : (5)

References (43)
  • 1
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: how close are the family ties?
    • Jentsch S, Pyrowolakis G, (2000) Ubiquitin and its kin: how close are the family ties? Trends Cell Biol 10: 335-342.
    • (2000) Trends Cell Biol , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 2
    • 32244446691 scopus 로고    scopus 로고
    • Mdy2, a ubiquitin-like (UBL)-domain protein, is required for efficient mating in Saccharomyces cerevisiae
    • Hu Z, Potthoff B, Hollenberg CP, Ramezani-Rad M, (2006) Mdy2, a ubiquitin-like (UBL)-domain protein, is required for efficient mating in Saccharomyces cerevisiae. J Cell Sci 119: 326-338.
    • (2006) J Cell Sci , vol.119 , pp. 326-338
    • Hu, Z.1    Potthoff, B.2    Hollenberg, C.P.3    Ramezani-Rad, M.4
  • 3
    • 0036295955 scopus 로고    scopus 로고
    • Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis
    • Saeki Y, Saitoh A, Toh-e A, Yokosawa H, (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293: 986-992.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 986-992
    • Saeki, Y.1    Saitoh, A.2    Toh-e, A.3    Yokosawa, H.4
  • 4
    • 78650318976 scopus 로고    scopus 로고
    • The yeast ubiquitin-like domain protein Mdy2 is required for microtubule-directed nuclear migration and localizes to cytoplasmic granules in response to heat stress
    • Cohnen A, Bielig H, Hollenberg CP, Hu Z, Ramezani-Rad M, (2010) The yeast ubiquitin-like domain protein Mdy2 is required for microtubule-directed nuclear migration and localizes to cytoplasmic granules in response to heat stress. Cytoskeleton (Hoboken) 67: 635-649.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 635-649
    • Cohnen, A.1    Bielig, H.2    Hollenberg, C.P.3    Hu, Z.4    Ramezani-Rad, M.5
  • 5
    • 0032842399 scopus 로고    scopus 로고
    • Disruption and functional analysis of six ORFs on chromosome XV: YOL117w, YOL115w (TRF4), YOL114c, YOL112w (MSB4), YOL111c and YOL072w
    • Iwanejko L, Smith KN, Loeillet S, Nicolas A, Fabre F, (1999) Disruption and functional analysis of six ORFs on chromosome XV: YOL117w, YOL115w (TRF4), YOL114c, YOL112w (MSB4), YOL111c and YOL072w. Yeast 15: 1529-1539.
    • (1999) Yeast , vol.15 , pp. 1529-1539
    • Iwanejko, L.1    Smith, K.N.2    Loeillet, S.3    Nicolas, A.4    Fabre, F.5
  • 6
    • 0023955912 scopus 로고
    • Expression of the G6PD locus on the human X chromosome is associated with demethylation of three CpG islands within 100 kb of DNA
    • Toniolo D, Martini G, Migeon BR, Dono R, (1988) Expression of the G6PD locus on the human X chromosome is associated with demethylation of three CpG islands within 100 kb of DNA. Embo J 7: 401-406.
    • (1988) Embo J , vol.7 , pp. 401-406
    • Toniolo, D.1    Martini, G.2    Migeon, B.R.3    Dono, R.4
  • 7
    • 77953245945 scopus 로고    scopus 로고
    • Automated identification of pathways from quantitative genetic interaction data
    • Battle A, Jonikas MC, Walter P, Weissman JS, Koller D, (2010) Automated identification of pathways from quantitative genetic interaction data. Mol Syst Biol 6: 379.
    • (2010) Mol Syst Biol , vol.6 , pp. 379
    • Battle, A.1    Jonikas, M.C.2    Walter, P.3    Weissman, J.S.4    Koller, D.5
  • 8
    • 75849130606 scopus 로고    scopus 로고
    • Structural insights into tail-anchored protein binding and membrane insertion by Get3
    • Bozkurt G, Stjepanovic G, Vilardi F, Amlacher S, Wild K, et al. (2009) Structural insights into tail-anchored protein binding and membrane insertion by Get3. Proc Natl Acad Sci U S A 106: 21131-21136.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21131-21136
    • Bozkurt, G.1    Stjepanovic, G.2    Vilardi, F.3    Amlacher, S.4    Wild, K.5
  • 10
    • 63449128473 scopus 로고    scopus 로고
    • Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum
    • Jonikas MC, Collins SR, Denic V, Oh E, Quan EM, et al. (2009) Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323: 1693-1697.
    • (2009) Science , vol.323 , pp. 1693-1697
    • Jonikas, M.C.1    Collins, S.R.2    Denic, V.3    Oh, E.4    Quan, E.M.5
  • 11
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • Wang F, Brown EC, Mak G, Zhuang J, Denic V, (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell 40: 159-171.
    • (2010) Mol Cell , vol.40 , pp. 159-171
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5
  • 12
  • 13
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich D, Kutay U, (1999) Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol 15: 607-660.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 14
    • 45149113882 scopus 로고    scopus 로고
    • A PY-NLS nuclear targeting signal is required for nuclear localization and function of the Saccharomyces cerevisiae mRNA-binding protein Hrp1
    • Lange A, Mills RE, Devine SE, Corbett AH, (2008) A PY-NLS nuclear targeting signal is required for nuclear localization and function of the Saccharomyces cerevisiae mRNA-binding protein Hrp1. J Biol Chem 283: 12926-12934.
    • (2008) J Biol Chem , vol.283 , pp. 12926-12934
    • Lange, A.1    Mills, R.E.2    Devine, S.E.3    Corbett, A.H.4
  • 15
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: definition, function, and interaction with importin alpha
    • Lange A, Mills RE, Lange CJ, Stewart M, Devine SE, et al. (2007) Classical nuclear localization signals: definition, function, and interaction with importin alpha. J Biol Chem 282: 5101-5105.
    • (2007) J Biol Chem , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5
  • 16
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: the soluble phase
    • Mattaj IW, Englmeier L, (1998) Nucleocytoplasmic transport: the soluble phase. Annu Rev Biochem 67: 265-306.
    • (1998) Annu Rev Biochem , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 17
    • 0025949412 scopus 로고
    • Nuclear targeting sequences-a consensus?
    • Dingwall C, Laskey RA, (1991) Nuclear targeting sequences-a consensus? Trends Biochem Sci 16: 478-481.
    • (1991) Trends Biochem Sci , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 18
    • 0021269089 scopus 로고
    • Sequence requirements for nuclear location of simian virus 40 large-T antigen
    • Kalderon D, Richardson WD, Markham AF, Smith AE, (1984) Sequence requirements for nuclear location of simian virus 40 large-T antigen. Nature 311: 33-38.
    • (1984) Nature , vol.311 , pp. 33-38
    • Kalderon, D.1    Richardson, W.D.2    Markham, A.F.3    Smith, A.E.4
  • 19
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence
    • Robbins J, Dilworth SM, Laskey RA, Dingwall C, (1991) Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell 64: 615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 20
    • 67349140506 scopus 로고    scopus 로고
    • Structural basis for leucine-rich nuclear export signal recognition by CRM1
    • Dong X, Biswas A, Suel KE, Jackson LK, Martinez R, et al. (2009) Structural basis for leucine-rich nuclear export signal recognition by CRM1. Nature 458: 1136-1141.
    • (2009) Nature , vol.458 , pp. 1136-1141
    • Dong, X.1    Biswas, A.2    Suel, K.E.3    Jackson, L.K.4    Martinez, R.5
  • 21
  • 22
    • 81855184492 scopus 로고    scopus 로고
    • Tail-anchored membrane protein insertion into the endoplasmic reticulum
    • Hegde RS, Keenan RJ, (2011) Tail-anchored membrane protein insertion into the endoplasmic reticulum. Nat Rev Mol Cell Biol 12: 787-798.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 787-798
    • Hegde, R.S.1    Keenan, R.J.2
  • 23
    • 77955499241 scopus 로고    scopus 로고
    • Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting
    • Simpson PJ, Schwappach B, Dohlman HG, Isaacson RL, (2010) Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting. Structure 18: 897-902.
    • (2010) Structure , vol.18 , pp. 897-902
    • Simpson, P.J.1    Schwappach, B.2    Dohlman, H.G.3    Isaacson, R.L.4
  • 24
  • 25
    • 84858027446 scopus 로고    scopus 로고
    • Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex
    • Chartron JW, VanderVelde DG, Rao M, Clemons WM, (2012) Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex. Journal of Biological Chemistry 287: 8310-8317.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 8310-8317
    • Chartron, J.W.1    VanderVelde, D.G.2    Rao, M.3    Clemons, W.M.4
  • 27
    • 77951209587 scopus 로고    scopus 로고
    • Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1
    • Chang YW, Chuang YC, Ho YC, Cheng MY, Sun YJ, et al. (2010) Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1. J Biol Chem 285: 9962-9970.
    • (2010) J Biol Chem , vol.285 , pp. 9962-9970
    • Chang, Y.W.1    Chuang, Y.C.2    Ho, Y.C.3    Cheng, M.Y.4    Sun, Y.J.5
  • 28
    • 80053210242 scopus 로고    scopus 로고
    • A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex
    • Chartron JW, Gonzalez GM, Clemons WM Jr, (2011) A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex. J Biol Chem 286: 34325-34334.
    • (2011) J Biol Chem , vol.286 , pp. 34325-34334
    • Chartron, J.W.1    Gonzalez, G.M.2    Clemons Jr., W.M.3
  • 29
    • 79251554956 scopus 로고    scopus 로고
    • Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae
    • Buchan JR, Yoon JH, Parker R, (2011) Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae. J Cell Sci 124: 228-239.
    • (2011) J Cell Sci , vol.124 , pp. 228-239
    • Buchan, J.R.1    Yoon, J.H.2    Parker, R.3
  • 30
    • 68949172267 scopus 로고    scopus 로고
    • Robust heat shock induces eIF2alpha-phosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae
    • Grousl T, Ivanov P, Frydlova I, Vasicova P, Janda F, et al. (2009) Robust heat shock induces eIF2alpha-phosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae. J Cell Sci 122: 2078-2088.
    • (2009) J Cell Sci , vol.122 , pp. 2078-2088
    • Grousl, T.1    Ivanov, P.2    Frydlova, I.3    Vasicova, P.4    Janda, F.5
  • 31
    • 34347387606 scopus 로고    scopus 로고
    • Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae
    • Brengues M, Parker R, (2007) Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae. Mol Biol Cell 18: 2592-2602.
    • (2007) Mol Biol Cell , vol.18 , pp. 2592-2602
    • Brengues, M.1    Parker, R.2
  • 32
    • 35348989809 scopus 로고    scopus 로고
    • Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies
    • Hoyle NP, Castelli LM, Campbell SG, Holmes LE, Ashe MP, (2007) Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies. J Cell Biol 179: 65-74.
    • (2007) J Cell Biol , vol.179 , pp. 65-74
    • Hoyle, N.P.1    Castelli, L.M.2    Campbell, S.G.3    Holmes, L.E.4    Ashe, M.P.5
  • 33
    • 15444366645 scopus 로고    scopus 로고
    • Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export
    • Brune C, Munchel SE, Fischer N, Podtelejnikov AV, Weis K, (2005) Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export. Rna 11: 517-531.
    • (2005) Rna , vol.11 , pp. 517-531
    • Brune, C.1    Munchel, S.E.2    Fischer, N.3    Podtelejnikov, A.V.4    Weis, K.5
  • 34
    • 33646537802 scopus 로고    scopus 로고
    • Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes
    • Fleischer TC, Weaver CM, McAfee KJ, Jennings JL, Link AJ, (2006) Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev 20: 1294-1307.
    • (2006) Genes Dev , vol.20 , pp. 1294-1307
    • Fleischer, T.C.1    Weaver, C.M.2    McAfee, K.J.3    Jennings, J.L.4    Link, A.J.5
  • 35
    • 34250862251 scopus 로고    scopus 로고
    • SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
    • Liou ST, Cheng MY, Wang C, (2007) SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae. Cell Stress Chaperones 12: 59-70.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 59-70
    • Liou, S.T.1    Cheng, M.Y.2    Wang, C.3
  • 36
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW, (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138: 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 37
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation
    • Wang Q, Liu Y, Soetandyo N, Baek K, Hegde R, et al. (2011) A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Mol Cell 42: 758-770.
    • (2011) Mol Cell , vol.42 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5
  • 39
    • 0036154218 scopus 로고    scopus 로고
    • Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules
    • Kedersha N, Chen S, Gilks N, Li W, Miller IJ, et al. (2002) Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules. Mol Biol Cell 13: 195-210.
    • (2002) Mol Biol Cell , vol.13 , pp. 195-210
    • Kedersha, N.1    Chen, S.2    Gilks, N.3    Li, W.4    Miller, I.J.5
  • 40
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: the ins and outs of translation
    • Buchan JR, Parker R, (2009) Eukaryotic stress granules: the ins and outs of translation. Mol Cell 36: 932-941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 41
    • 22344455246 scopus 로고    scopus 로고
    • Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
    • Kedersha N, Stoecklin G, Ayodele M, Yacono P, Lykke-Andersen J, et al. (2005) Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J Cell Biol 169: 871-884.
    • (2005) J Cell Biol , vol.169 , pp. 871-884
    • Kedersha, N.1    Stoecklin, G.2    Ayodele, M.3    Yacono, P.4    Lykke-Andersen, J.5
  • 42
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • Arimoto K, Fukuda H, Imajoh-Ohmi S, Saito H, Takekawa M, (2008) Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat Cell Biol 10: 1324-1332.
    • (2008) Nat Cell Biol , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.