메뉴 건너뛰기




Volumn 8, Issue 6, 2013, Pages

Involvement of MoVMA11, a Putative Vacuolar ATPase c' Subunit, in Vacuolar Acidification and Infection-Related Morphogenesis of Magnaporthe oryzae

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CALCIUM; HEAVY METAL; MEPACRINE; MUTANT PROTEIN; UNCLASSIFIED DRUG; VACUOLAR ADENOSINE TRIPHOSPHATASE; FUNGAL PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84879524018     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0067804     Document Type: Article
Times cited : (20)

References (70)
  • 1
    • 0032946360 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton-adenosinetriphosphatases
    • 10221984
    • Nelson N, Harvey WR, (1999) Vacuolar and plasma membrane proton-adenosinetriphosphatases. Physiol Rev 79: 361-385. PubMed: 10221984.
    • (1999) Physiol Rev , vol.79 , pp. 361-385
    • Nelson, N.1    Harvey, W.R.2
  • 2
    • 0142120596 scopus 로고    scopus 로고
    • Structure and assembly of the yeast V-ATPase
    • 10.1023/A:1025772730586
    • Graham LA, Flannery AR, Stevens TH, (2003) Structure and assembly of the yeast V-ATPase. J Bioenerg Biomembr 35: 301-312. doi:10.1023/A:1025772730586. PubMed: 14635776.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 301-312
    • Graham, L.A.1    Flannery, A.R.2    Stevens, T.H.3
  • 3
    • 0033974290 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H(+)-ATPase
    • 10600676
    • Kane PM, Parra KJ, (2000) Assembly and regulation of the yeast vacuolar H(+)-ATPase. J Exp Biol 203: 81-87. PubMed: 10600676.
    • (2000) J Exp Biol , vol.203 , pp. 81-87
    • Kane, P.M.1    Parra, K.J.2
  • 4
    • 77955405903 scopus 로고    scopus 로고
    • Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase
    • 10.1038/emboj.2010.138
    • Dechant R, Binda M, Lee SS, Pelet S, Winderickx J, et al. (2010) Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase. EMBO J 29: 2515-2526. doi:10.1038/emboj.2010.138. PubMed: 20581803.
    • (2010) EMBO J , vol.29 , pp. 2515-2526
    • Dechant, R.1    Binda, M.2    Lee, S.S.3    Pelet, S.4    Winderickx, J.5
  • 5
    • 84856022796 scopus 로고    scopus 로고
    • Evolution of increased complexity in a molecular machine
    • 22230956
    • Finnigan GC, Hanson-Smith V, Stevens TH, Thornton JW, (2012) Evolution of increased complexity in a molecular machine. Nature 481: 360-364. PubMed: 22230956.
    • (2012) Nature , vol.481 , pp. 360-364
    • Finnigan, G.C.1    Hanson-Smith, V.2    Stevens, T.H.3    Thornton, J.W.4
  • 6
    • 0034604676 scopus 로고    scopus 로고
    • Molecular characterization of the yeast vacuolar H+-ATPase proton pore
    • 10.1074/jbc.M004440200
    • Powell B, Graham LA, Stevens TH, (2000) Molecular characterization of the yeast vacuolar H+-ATPase proton pore. J Biol Chem 275: 23654-23660. doi:10.1074/jbc.M004440200. PubMed: 10825180.
    • (2000) J Biol Chem , vol.275 , pp. 23654-23660
    • Powell, B.1    Graham, L.A.2    Stevens, T.H.3
  • 7
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
    • 10.1038/nrm2272
    • Forgac M, (2007) Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat Rev Mol Cell Biol 8: 917-929. doi:10.1038/nrm2272. PubMed: 17912264.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 917-929
    • Forgac, M.1
  • 8
    • 33645119556 scopus 로고    scopus 로고
    • The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase
    • 10.1128/MMBR.70.1.177-191.2006
    • Kane PM, (2006) The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase. Microbiol Mol Biol Rev 70: 177-191. doi:10.1128/MMBR.70.1.177-191.2006. PubMed: 16524922.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 177-191
    • Kane, P.M.1
  • 9
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases--nature's most versatile proton pumps
    • 10.1038/nrm729
    • Nishi T, Forgac M, (2002) The vacuolar (H+)-ATPases--nature's most versatile proton pumps. Nat Rev Mol Cell Biol 3: 94-103. doi:10.1038/nrm729. PubMed: 11836511.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 10
    • 0025358278 scopus 로고
    • Disruption of genes encoding subunits of yeast vacuolar H(+)-ATPase causes conditional lethality
    • 10.1073/pnas.87.9.3503
    • Nelson H, Nelson N, (1990) Disruption of genes encoding subunits of yeast vacuolar H(+)-ATPase causes conditional lethality. Proc Natl Acad Sci U S A 87: 3503-3507. doi:10.1073/pnas.87.9.3503. PubMed: 2139726.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 3503-3507
    • Nelson, H.1    Nelson, N.2
  • 11
    • 0025879774 scopus 로고
    • Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H(+)-ATPase activity
    • 1830311
    • Ohya Y, Umemoto N, Tanida I, Ohta A, Iida H, et al. (1991) Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H(+)-ATPase activity. J Biol Chem 266: 13971-13977. PubMed: 1830311.
    • (1991) J Biol Chem , vol.266 , pp. 13971-13977
    • Ohya, Y.1    Umemoto, N.2    Tanida, I.3    Ohta, A.4    Iida, H.5
  • 12
    • 1842787818 scopus 로고    scopus 로고
    • Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting
    • 10.1007/s00438-003-0971-7
    • Iwaki T, Goa T, Tanaka N, Takegawa K, (2004) Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting. Mol Genet Genomics 271: 197-207. doi:10.1007/s00438-003-0971-7. PubMed: 14735354.
    • (2004) Mol Genet Genomics , vol.271 , pp. 197-207
    • Iwaki, T.1    Goa, T.2    Tanaka, N.3    Takegawa, K.4
  • 13
    • 19044365896 scopus 로고    scopus 로고
    • The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence
    • 10.1099/mic.0.27505-0
    • Poltermann S, Nguyen M, Günther J, Wendland J, Härtl A, et al. (2005) The putative vacuolar ATPase subunit Vma7p of Candida albicans is involved in vacuole acidification, hyphal development and virulence. Microbiology 151: 1645-1655. doi:10.1099/mic.0.27505-0. PubMed: 15870472.
    • (2005) Microbiology , vol.151 , pp. 1645-1655
    • Poltermann, S.1    Nguyen, M.2    Günther, J.3    Wendland, J.4    Härtl, A.5
  • 14
    • 0034614496 scopus 로고    scopus 로고
    • Disruption of vma-1, the gene encoding the catalytic subunit of the vacuolar H(+)-ATPase, causes severe morphological changes in Neurospora crassa
    • 10.1074/jbc.275.1.167
    • Bowman EJ, Kendle R, Bowman BJ, (2000) Disruption of vma-1, the gene encoding the catalytic subunit of the vacuolar H(+)-ATPase, causes severe morphological changes in Neurospora crassa. J Biol Chem 275: 167-176. doi:10.1074/jbc.275.1.167. PubMed: 10617601.
    • (2000) J Biol Chem , vol.275 , pp. 167-176
    • Bowman, E.J.1    Kendle, R.2    Bowman, B.J.3
  • 15
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • 10.1021/bi100397s
    • Toei M, Saum R, Forgac M, (2010) Regulation and isoform function of the V-ATPases. Biochemistry 49: 4715-4723. doi:10.1021/bi100397s. PubMed: 20450191.
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 16
    • 0033973341 scopus 로고    scopus 로고
    • Composition and assembly of the yeast vacuolar H(+)-ATPase complex
    • 10600674
    • Graham LA, Powell B, Stevens TH, (2000) Composition and assembly of the yeast vacuolar H(+)-ATPase complex. J Exp Biol 203: 61-70. PubMed: 10600674.
    • (2000) J Exp Biol , vol.203 , pp. 61-70
    • Graham, L.A.1    Powell, B.2    Stevens, T.H.3
  • 17
    • 20244366844 scopus 로고    scopus 로고
    • The genome sequence of the rice blast fungus Magnaporthe grisea
    • 10.1038/nature03449
    • Dean RA, Talbot NJ, Ebbole DJ, Farman ML, Mitchell TK, et al. (2005) The genome sequence of the rice blast fungus Magnaporthe grisea. Nature 434: 980-986. doi:10.1038/nature03449. PubMed: 15846337.
    • (2005) Nature , vol.434 , pp. 980-986
    • Dean, R.A.1    Talbot, N.J.2    Ebbole, D.J.3    Farman, M.L.4    Mitchell, T.K.5
  • 18
    • 0038275922 scopus 로고    scopus 로고
    • The rice blast pathosystem as a case study for the development of new tools and raw materials for genome analysis of fungal plant pathogens
    • 10.1046/j.1469-8137.2003.00787.x
    • Mitchell TK, Thon MR, Jeong JS, Brown D, Deng JX, et al. (2003) The rice blast pathosystem as a case study for the development of new tools and raw materials for genome analysis of fungal plant pathogens. New Phytol 159: 53-61. doi:10.1046/j.1469-8137.2003.00787.x.
    • (2003) New Phytol , vol.159 , pp. 53-61
    • Mitchell, T.K.1    Thon, M.R.2    Jeong, J.S.3    Brown, D.4    Deng, J.X.5
  • 19
    • 35148848640 scopus 로고    scopus 로고
    • Magnaporthe as a model for understanding host-pathogen interactions
    • 10.1146/annurev.phyto.45.062806.094346
    • Ebbole DJ, (2007) Magnaporthe as a model for understanding host-pathogen interactions. Annu Rev Phytopathol 45: 437-456. doi:10.1146/annurev.phyto.45.062806.094346. PubMed: 17489691.
    • (2007) Annu Rev Phytopathol , vol.45 , pp. 437-456
    • Ebbole, D.J.1
  • 20
    • 0242693135 scopus 로고    scopus 로고
    • On the trail of a cereal killer: Exploring the biology of Magnaporthe grisea
    • 10.1146/annurev.micro.57.030502.090957
    • Talbot NJ, (2003) On the trail of a cereal killer: Exploring the biology of Magnaporthe grisea. Annu Rev Microbiol 57: 177-202. doi:10.1146/annurev.micro.57.030502.090957. PubMed: 14527276.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 177-202
    • Talbot, N.J.1
  • 21
    • 60749094240 scopus 로고    scopus 로고
    • Under pressure: investigating the biology of plant infection by Magnaporthe oryzae
    • 10.1038/nrmicro2032
    • Wilson RA, Talbot NJ, (2009) Under pressure: investigating the biology of plant infection by Magnaporthe oryzae. Nat Rev Microbiol 7: 185-195. doi:10.1038/nrmicro2032. PubMed: 19219052.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 185-195
    • Wilson, R.A.1    Talbot, N.J.2
  • 22
    • 0029846423 scopus 로고    scopus 로고
    • MAP kinase and cAMP signaling regulate infection structure formation and pathogenic growth in the rice blast fungus Magnaporthe grisea
    • 10.1101/gad.10.21.2696
    • Xu JR, Hamer JE, (1996) MAP kinase and cAMP signaling regulate infection structure formation and pathogenic growth in the rice blast fungus Magnaporthe grisea. Genes Dev 10: 2696-2706. doi:10.1101/gad.10.21.2696. PubMed: 8946911.
    • (1996) Genes Dev , vol.10 , pp. 2696-2706
    • Xu, J.R.1    Hamer, J.E.2
  • 23
    • 0031278132 scopus 로고    scopus 로고
    • The adenylate cyclase gene MAC1 of Magnaporthe grisea controls appressorium formation and other aspects of growth and development
    • 10.2307/3870558
    • Choi W, Dean RA, (1997) The adenylate cyclase gene MAC1 of Magnaporthe grisea controls appressorium formation and other aspects of growth and development. Plant Cell 9: 1973-1983. doi:10.2307/3870558. PubMed: 9401122.
    • (1997) Plant Cell , vol.9 , pp. 1973-1983
    • Choi, W.1    Dean, R.A.2
  • 24
    • 0033785089 scopus 로고    scopus 로고
    • MAP kinase and protein kinase A-dependent mobilization of triacylglycerol and glycogen during appressorium turgor generation by Magnaporthe grisea
    • 10.2307/3871184
    • Thines E, Weber RW, Talbot NJ, (2000) MAP kinase and protein kinase A-dependent mobilization of triacylglycerol and glycogen during appressorium turgor generation by Magnaporthe grisea. Plant Cell 12: 1703-1718. doi:10.2307/3871184. PubMed: 11006342.
    • (2000) Plant Cell , vol.12 , pp. 1703-1718
    • Thines, E.1    Weber, R.W.2    Talbot, N.J.3
  • 25
    • 0025170681 scopus 로고
    • The fungal vacuole: composition, function, and biogenesis
    • 2215422
    • Klionsky DJ, Herman PK, Emr SD, (1990) The fungal vacuole: composition, function, and biogenesis. Microbiol Rev 54: 266-292. PubMed: 2215422.
    • (1990) Microbiol Rev , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 26
    • 56949088879 scopus 로고    scopus 로고
    • Vacuoles and fungal biology
    • 10.1016/j.mib.2008.09.017
    • Veses V, Richards A, Gow NA, (2008) Vacuoles and fungal biology. Curr Opin Microbiol 11: 503-510. doi:10.1016/j.mib.2008.09.017. PubMed: 18935977.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 503-510
    • Veses, V.1    Richards, A.2    Gow, N.A.3
  • 27
    • 0035048338 scopus 로고    scopus 로고
    • The vacuole as central element of the lytic system and sink for lipid droplets in maturing appressoria of Magnaporthe grisea
    • 10.1007/BF02680137
    • Weber RW, Wakley GE, Thines E, Talbot NJ, (2001) The vacuole as central element of the lytic system and sink for lipid droplets in maturing appressoria of Magnaporthe grisea. Protoplasma 216: 101-112. doi:10.1007/BF02680137. PubMed: 11732192.
    • (2001) Protoplasma , vol.216 , pp. 101-112
    • Weber, R.W.1    Wakley, G.E.2    Thines, E.3    Talbot, N.J.4
  • 28
    • 33646242045 scopus 로고    scopus 로고
    • Autophagic fungal cell death is necessary for infection by the rice blast fungus
    • 10.1126/science.1124550
    • Veneault-Fourrey C, Barooah M, Egan M, Wakley G, Talbot NJ, (2006) Autophagic fungal cell death is necessary for infection by the rice blast fungus. Science 312: 580-583. doi:10.1126/science.1124550. PubMed: 16645096.
    • (2006) Science , vol.312 , pp. 580-583
    • Veneault-Fourrey, C.1    Barooah, M.2    Egan, M.3    Wakley, G.4    Talbot, N.J.5
  • 29
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: molecular mechanisms and biological functions of autophagy
    • 10.1016/S1534-5807(04)00099-1
    • Levine B, Klionsky DJ, (2004) Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell 6: 463-477. doi:10.1016/S1534-5807(04)00099-1. PubMed: 15068787.
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 30
    • 34250798552 scopus 로고    scopus 로고
    • Involvement of a Magnaporthe grisea serine/threonine kinase gene, MgATG1, in appressorium turgor and pathogenesis
    • 10.1128/EC.00011-07
    • Liu XH, Lu JP, Zhang L, Dong B, Min H, et al. (2007) Involvement of a Magnaporthe grisea serine/threonine kinase gene, MgATG1, in appressorium turgor and pathogenesis. Eukaryot Cell 6: 997-1005. doi:10.1128/EC.00011-07. PubMed: 17416896.
    • (2007) Eukaryot Cell , vol.6 , pp. 997-1005
    • Liu, X.H.1    Lu, J.P.2    Zhang, L.3    Dong, B.4    Min, H.5
  • 31
    • 40649103950 scopus 로고    scopus 로고
    • Rice blast infection of Brachypodium distachyon as a model system to study dynamic host/pathogen interactions
    • 10.1038/nprot.2007.499
    • Parker D, Beckmann M, Enot DP, Overy DP, Rios ZC, et al. (2008) Rice blast infection of Brachypodium distachyon as a model system to study dynamic host/pathogen interactions. Nat Protoc 3: 435-445. doi:10.1038/nprot.2007.499. PubMed: 18323815.
    • (2008) Nat Protoc , vol.3 , pp. 435-445
    • Parker, D.1    Beckmann, M.2    Enot, D.P.3    Overy, D.P.4    Rios, Z.C.5
  • 32
    • 0025976160 scopus 로고
    • Magnaporthe grisea genes for pathogenicity and virulence identified through a series of backcrosses
    • 2016048
    • Valent B, Farrall L, Chumley FG, (1991) Magnaporthe grisea genes for pathogenicity and virulence identified through a series of backcrosses. Genetics 127: 87-101. PubMed: 2016048.
    • (1991) Genetics , vol.127 , pp. 87-101
    • Valent, B.1    Farrall, L.2    Chumley, F.G.3
  • 33
    • 53549098810 scopus 로고    scopus 로고
    • A simple and effective method for total RNA isolation of appressoria in Magnaporthe oryzae
    • 10.1631/jzus.B0860011
    • Liu TB, Lu JP, Liu XH, Min H, Lin FC, (2008) A simple and effective method for total RNA isolation of appressoria in Magnaporthe oryzae. J Zhejiang Univ Sci B 9: 811-817. doi:10.1631/jzus.B0860011. PubMed: 18837109.
    • (2008) J Zhejiang Univ Sci B , vol.9 , pp. 811-817
    • Liu, T.B.1    Lu, J.P.2    Liu, X.H.3    Min, H.4    Lin, F.C.5
  • 34
    • 84877000180 scopus 로고    scopus 로고
    • MoMon1 is required for vacuolar assembly, conidiogenesis and pathogenicity in the rice blast fungus Magnaporthe oryzae
    • 10.1016/j.resmic.2013.01.001
    • Gao HM, Liu XG, Shi HB, Lu JP, Yang J, et al. (2013) MoMon1 is required for vacuolar assembly, conidiogenesis and pathogenicity in the rice blast fungus Magnaporthe oryzae. Res Microbiol 164: 300-309. doi:10.1016/j.resmic.2013.01.001. PubMed: 23376292.
    • (2013) Res Microbiol , vol.164 , pp. 300-309
    • Gao, H.M.1    Liu, X.G.2    Shi, H.B.3    Lu, J.P.4    Yang, J.5
  • 35
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • 10.1006/meth.2001.1262
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402-408. doi:10.1006/meth.2001.1262. PubMed: 11846609.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 36
    • 4644220750 scopus 로고    scopus 로고
    • Double-joint PCR: a PCR-based molecular tool for gene manipulations in filamentous fungi
    • 10.1016/j.fgb.2004.08.001
    • Yu JH, Hamari Z, Han KH, Seo JA, Reyes-Domínguez Y, et al. (2004) Double-joint PCR: a PCR-based molecular tool for gene manipulations in filamentous fungi. Fungal Genet Biol 41: 973-981. doi:10.1016/j.fgb.2004.08.001. PubMed: 15465386.
    • (2004) Fungal Genet Biol , vol.41 , pp. 973-981
    • Yu, J.H.1    Hamari, Z.2    Han, K.H.3    Seo, J.A.4    Reyes-Domínguez, Y.5
  • 37
    • 0035981212 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens-mediated transformation of the plant pathogenic fungus, Magnaporthe grisea
    • 11804343
    • Rho HS, Kang S, Lee YH, (2001) Agrobacterium tumefaciens-mediated transformation of the plant pathogenic fungus, Magnaporthe grisea. Mol Cells 12: 407-411. PubMed: 11804343.
    • (2001) Mol Cells , vol.12 , pp. 407-411
    • Rho, H.S.1    Kang, S.2    Lee, Y.H.3
  • 38
    • 0036438765 scopus 로고    scopus 로고
    • Live-cell imaging of endocytosis during conidial germination in the rice blast fungus, Magnaporthe grisea
    • 10.1016/S1087-1845(02)00535-2
    • Atkinson HA, Daniels A, Read ND, (2002) Live-cell imaging of endocytosis during conidial germination in the rice blast fungus, Magnaporthe grisea. Fungal Genet Biol 37: 233-244. doi:10.1016/S1087-1845(02)00535-2. PubMed: 12431458.
    • (2002) Fungal Genet Biol , vol.37 , pp. 233-244
    • Atkinson, H.A.1    Daniels, A.2    Read, N.D.3
  • 39
    • 0036389847 scopus 로고    scopus 로고
    • Visualization of vacuoles in Aspergillus oryzae by expression of CPY-EGFP
    • 10.1016/S1087-1845(02)00033-6
    • Ohneda M, Arioka M, Nakajima H, Kitamoto K, (2002) Visualization of vacuoles in Aspergillus oryzae by expression of CPY-EGFP. Fungal Genet Biol 37: 29-38. doi:10.1016/S1087-1845(02)00033-6. PubMed: 12223187.
    • (2002) Fungal Genet Biol , vol.37 , pp. 29-38
    • Ohneda, M.1    Arioka, M.2    Nakajima, H.3    Kitamoto, K.4
  • 40
    • 0023432180 scopus 로고
    • Multiple methods of visualizing the yeast vacuole permit evaluation of its morphology and inheritance during the cell cycle
    • 10.1083/jcb.105.4.1539
    • Weisman LS, Bacallao R, Wickner W, (1987) Multiple methods of visualizing the yeast vacuole permit evaluation of its morphology and inheritance during the cell cycle. J Cell Biol 105: 1539-1547. doi:10.1083/jcb.105.4.1539. PubMed: 2444598.
    • (1987) J Cell Biol , vol.105 , pp. 1539-1547
    • Weisman, L.S.1    Bacallao, R.2    Wickner, W.3
  • 41
    • 59449088040 scopus 로고    scopus 로고
    • Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum
    • 10.1091/mbc.E08-06-0629
    • Ryan M, Graham LA, Stevens TH, (2008) Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum. Mol Biol Cell 19: 5131-5142. doi:10.1091/mbc.E08-06-0629. PubMed: 18799613.
    • (2008) Mol Biol Cell , vol.19 , pp. 5131-5142
    • Ryan, M.1    Graham, L.A.2    Stevens, T.H.3
  • 42
    • 58149389726 scopus 로고    scopus 로고
    • Autophagy-assisted glycogen catabolism regulates asexual differentiation in Magnaporthe oryzae
    • 10.4161/auto.5.1.7175
    • Deng YZ, Ramos-Pamplona M, Naqvi NI, (2009) Autophagy-assisted glycogen catabolism regulates asexual differentiation in Magnaporthe oryzae. Autophagy 5: 33-43. doi:10.4161/auto.5.1.7175. PubMed: 19115483.
    • (2009) Autophagy , vol.5 , pp. 33-43
    • Deng, Y.Z.1    Ramos-Pamplona, M.2    Naqvi, N.I.3
  • 43
    • 0032098394 scopus 로고    scopus 로고
    • Acropetal: a genetic locus required for conidiophore architecture and pathogenicity in the rice blast fungus
    • 10.1006/fgbi.1998.1053
    • Lau GW, Hamer JE, (1998) Acropetal: a genetic locus required for conidiophore architecture and pathogenicity in the rice blast fungus. Fungal Genet Biol 24: 228-239. doi:10.1006/fgbi.1998.1053. PubMed: 9742203.
    • (1998) Fungal Genet Biol , vol.24 , pp. 228-239
    • Lau, G.W.1    Hamer, J.E.2
  • 44
    • 34248562159 scopus 로고    scopus 로고
    • Fusion PCR and gene targeting in Aspergillus nidulans
    • 17406574
    • Szewczyk E, Nayak T, Oakley CE, Edgerton H, Xiong Y, et al. (2006) Fusion PCR and gene targeting in Aspergillus nidulans. Nat Protoc 1: 3111-3120. PubMed: 17406574.
    • (2006) Nat Protoc , vol.1 , pp. 3111-3120
    • Szewczyk, E.1    Nayak, T.2    Oakley, C.E.3    Edgerton, H.4    Xiong, Y.5
  • 45
    • 73349129035 scopus 로고    scopus 로고
    • Structure and distribution of organelles and cellular location of calcium transporters in Neurospora crassa
    • 10.1128/EC.00174-09
    • Bowman BJ, Draskovic M, Freitag M, Bowman EJ, (2009) Structure and distribution of organelles and cellular location of calcium transporters in Neurospora crassa. Eukaryot Cell 8: 1845-1855. doi:10.1128/EC.00174-09. PubMed: 19801418.
    • (2009) Eukaryot Cell , vol.8 , pp. 1845-1855
    • Bowman, B.J.1    Draskovic, M.2    Freitag, M.3    Bowman, E.J.4
  • 46
    • 1642372806 scopus 로고    scopus 로고
    • FM-dyes as experimental probes for dissecting vesicle trafficking in living plant cells
    • 10.1111/j.0022-2720.2004.01348.x
    • Bolte S, Talbot C, Boutte Y, Catrice O, Read ND, et al. (2004) FM-dyes as experimental probes for dissecting vesicle trafficking in living plant cells. J Microsc 214: 159-173. doi:10.1111/j.0022-2720.2004.01348.x. PubMed: 15102063.
    • (2004) J Microsc , vol.214 , pp. 159-173
    • Bolte, S.1    Talbot, C.2    Boutte, Y.3    Catrice, O.4    Read, N.D.5
  • 47
    • 33748748342 scopus 로고    scopus 로고
    • Analysis of strains with mutations in six genes encoding subunits of the V-ATPase: eukaryotes differ in the composition of the V0 sector of the enzyme
    • 10.1074/jbc.M603883200
    • Chavez C, Bowman EJ, Reidling JC, Haw KH, Bowman BJ, (2006) Analysis of strains with mutations in six genes encoding subunits of the V-ATPase: eukaryotes differ in the composition of the V0 sector of the enzyme. J Biol Chem 281: 27052-27062. doi:10.1074/jbc.M603883200. PubMed: 16857684.
    • (2006) J Biol Chem , vol.281 , pp. 27052-27062
    • Chavez, C.1    Bowman, E.J.2    Reidling, J.C.3    Haw, K.H.4    Bowman, B.J.5
  • 48
    • 77749292435 scopus 로고    scopus 로고
    • Alkali metal cation transport and homeostasis in yeasts
    • 10.1128/MMBR.00042-09
    • Ariño J, Ramos J, Sychrová H, (2010) Alkali metal cation transport and homeostasis in yeasts. Microbiol Mol Biol Rev 74: 95-120. doi:10.1128/MMBR.00042-09. PubMed: 20197501.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 95-120
    • Ariño, J.1    Ramos, J.2    Sychrová, H.3
  • 49
    • 0027508062 scopus 로고
    • The vacuolar H(+)-ATPase of Saccharomyces cerevisiae is required for efficient copper detoxification, mitochondrial function, and iron metabolism
    • 8246899
    • Eide DJ, Bridgham JT, Zhao Z, Mattoon JR, (1993) The vacuolar H(+)-ATPase of Saccharomyces cerevisiae is required for efficient copper detoxification, mitochondrial function, and iron metabolism. Mol Gen Genet 241: 447-456. PubMed: 8246899.
    • (1993) Mol Gen Genet , vol.241 , pp. 447-456
    • Eide, D.J.1    Bridgham, J.T.2    Zhao, Z.3    Mattoon, J.R.4
  • 50
    • 25444459083 scopus 로고    scopus 로고
    • A genomic screen for yeast vacuolar membrane ATPase mutants
    • 10.1534/genetics.105.042812
    • Sambade M, Alba M, Smardon AM, West RW, Kane PM, (2005) A genomic screen for yeast vacuolar membrane ATPase mutants. Genetics 170: 1539-1551. doi:10.1534/genetics.105.042812. PubMed: 15937126.
    • (2005) Genetics , vol.170 , pp. 1539-1551
    • Sambade, M.1    Alba, M.2    Smardon, A.M.3    West, R.W.4    Kane, P.M.5
  • 51
    • 84860910461 scopus 로고    scopus 로고
    • Different chitin synthase genes are required for various developmental and plant infection processes in the rice blast fungus Magnaporthe oryzae
    • 22346755
    • Kong LA, Yang J, Li GT, Qi LL, Zhang YJ, et al. (2012) Different chitin synthase genes are required for various developmental and plant infection processes in the rice blast fungus Magnaporthe oryzae. PLOS Pathog 8: e1002526. PubMed: 22346755.
    • (2012) PLOS Pathog , vol.8
    • Kong, L.A.1    Yang, J.2    Li, G.T.3    Qi, L.L.4    Zhang, Y.J.5
  • 52
    • 0035166540 scopus 로고    scopus 로고
    • Multiple virulence factors of Cryptococcus neoformans are dependent on VPH1
    • 10.1046/j.1365-2958.2001.02712.x
    • Erickson T, Liu L, Gueyikian A, Zhu X, Gibbons J, et al. (2001) Multiple virulence factors of Cryptococcus neoformans are dependent on VPH1. Mol Microbiol 42: 1121-1131. doi:10.1046/j.1365-2958.2001.02712.x. PubMed: 11737651.
    • (2001) Mol Microbiol , vol.42 , pp. 1121-1131
    • Erickson, T.1    Liu, L.2    Gueyikian, A.3    Zhu, X.4    Gibbons, J.5
  • 53
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • 10.1038/nature02026
    • Huh WK, Falvo JV, Gerke LC, Carroll AS, Howson RW, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425: 686-691. doi:10.1038/nature02026. PubMed: 14562095.
    • (2003) Nature , vol.425 , pp. 686-691
    • Huh, W.K.1    Falvo, J.V.2    Gerke, L.C.3    Carroll, A.S.4    Howson, R.W.5
  • 54
    • 0031040410 scopus 로고    scopus 로고
    • VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase
    • 10.1074/jbc.272.8.4795
    • Hirata R, Graham LA, Takatsuki A, Stevens TH, Anraku Y, (1997) VMA11 and VMA16 encode second and third proteolipid subunits of the Saccharomyces cerevisiae vacuolar membrane H+-ATPase. J Biol Chem 272: 4795-4803. doi:10.1074/jbc.272.8.4795. PubMed: 9030535.
    • (1997) J Biol Chem , vol.272 , pp. 4795-4803
    • Hirata, R.1    Graham, L.A.2    Takatsuki, A.3    Stevens, T.H.4    Anraku, Y.5
  • 55
    • 4544289322 scopus 로고    scopus 로고
    • Topological characterization of the c, c', and c″ subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae
    • 10.1074/jbc.M406767200
    • Flannery AR, Graham LA, Stevens TH, (2004) Topological characterization of the c, c', and c″ subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae. J Biol Chem 279: 39856-39862. doi:10.1074/jbc.M406767200. PubMed: 15252052.
    • (2004) J Biol Chem , vol.279 , pp. 39856-39862
    • Flannery, A.R.1    Graham, L.A.2    Stevens, T.H.3
  • 56
    • 50649120655 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast
    • 10.1074/jbc.M710470200
    • Martínez-Muñoz GA, Kane P, (2008) Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast. J Biol Chem 283: 20309-20319. doi:10.1074/jbc.M710470200. PubMed: 18502746.
    • (2008) J Biol Chem , vol.283 , pp. 20309-20319
    • Martínez-Muñoz, G.A.1    Kane, P.2
  • 57
    • 33645294005 scopus 로고    scopus 로고
    • A P-type ATPase required for rice blast disease and induction of host resistance
    • 10.1038/nature04567
    • Gilbert MJ, Thornton CR, Wakley GE, Talbot NJ, (2006) A P-type ATPase required for rice blast disease and induction of host resistance. Nature 440: 535-539. doi:10.1038/nature04567. PubMed: 16554820.
    • (2006) Nature , vol.440 , pp. 535-539
    • Gilbert, M.J.1    Thornton, C.R.2    Wakley, G.E.3    Talbot, N.J.4
  • 58
    • 1642308586 scopus 로고    scopus 로고
    • Disruption of the gene encoding the V-ATPase subunit A results in inhibition of normal growth and abolished sporulation in Aspergillus nidulans
    • 10.1099/mic.0.26807-0
    • Melin P, Schnürer J, Wagner EG, (2004) Disruption of the gene encoding the V-ATPase subunit A results in inhibition of normal growth and abolished sporulation in Aspergillus nidulans. Microbiology 150: 743-748. doi:10.1099/mic.0.26807-0. PubMed: 14993324.
    • (2004) Microbiology , vol.150 , pp. 743-748
    • Melin, P.1    Schnürer, J.2    Wagner, E.G.3
  • 59
    • 84859002520 scopus 로고    scopus 로고
    • Vacuolar H(+)-ATPase plays a key role in cell wall biosynthesis of Aspergillus niger
    • 10.1016/j.fgb.2011.12.008
    • Schachtschabel D, Arentshorst M, Lagendijk EL, Ram AF, (2012) Vacuolar H(+)-ATPase plays a key role in cell wall biosynthesis of Aspergillus niger. Fungal Genet Biol 49: 284-293. doi:10.1016/j.fgb.2011.12.008. PubMed: 22222772.
    • (2012) Fungal Genet Biol , vol.49 , pp. 284-293
    • Schachtschabel, D.1    Arentshorst, M.2    Lagendijk, E.L.3    Ram, A.F.4
  • 60
    • 0037046286 scopus 로고    scopus 로고
    • Cloning and characterization of vmaA, the gene encoding a 69-kDa catalytic subunit of the vacuolar H+-ATPase during alkaline pH mediated growth of Aspergillus oryzae
    • 10.1111/j.1574-6968.2002.tb11144.x
    • Kuroki Y, Juvvadi PR, Arioka M, Nakajima H, Kitamoto K, (2002) Cloning and characterization of vmaA, the gene encoding a 69-kDa catalytic subunit of the vacuolar H+-ATPase during alkaline pH mediated growth of Aspergillus oryzae. FEMS Microbiol Lett 209: 277-282. doi:10.1111/j.1574-6968.2002.tb11144.x. PubMed: 12007818.
    • (2002) FEMS Microbiol Lett , vol.209 , pp. 277-282
    • Kuroki, Y.1    Juvvadi, P.R.2    Arioka, M.3    Nakajima, H.4    Kitamoto, K.5
  • 61
    • 0037940408 scopus 로고    scopus 로고
    • Physiological consequence of disruption of the VMA1 gene in the riboflavin overproducer Ashbya gossypii
    • 10.1074/jbc.274.14.9442
    • Förster C, Santos MA, Ruffert S, Krämer R, Revuelta JL, (1999) Physiological consequence of disruption of the VMA1 gene in the riboflavin overproducer Ashbya gossypii. J Biol Chem 274: 9442-9448. doi:10.1074/jbc.274.14.9442. PubMed: 10092625.
    • (1999) J Biol Chem , vol.274 , pp. 9442-9448
    • Förster, C.1    Santos, M.A.2    Ruffert, S.3    Krämer, R.4    Revuelta, J.L.5
  • 62
    • 1042278165 scopus 로고    scopus 로고
    • Genome-wide analysis of iron-dependent growth reveals a novel yeast gene required for vacuolar acidification
    • 14594803
    • Davis-Kaplan SR, Ward DM, Shiflett SL, Kaplan J, (2004) Genome-wide analysis of iron-dependent growth reveals a novel yeast gene required for vacuolar acidification. J Biol Chem 279: 4322-4329. PubMed: 14594803.
    • (2004) J Biol Chem , vol.279 , pp. 4322-4329
    • Davis-Kaplan, S.R.1    Ward, D.M.2    Shiflett, S.L.3    Kaplan, J.4
  • 63
    • 0030668723 scopus 로고    scopus 로고
    • Cryptococcus neoformans mating and virulence are regulated by the G-protein alpha subunit GPA1 and cAMP
    • 10.1101/gad.11.23.3206
    • Alspaugh JA, Perfect JR, Heitman J, (1997) Cryptococcus neoformans mating and virulence are regulated by the G-protein alpha subunit GPA1 and cAMP. Genes Dev 11: 3206-3217. doi:10.1101/gad.11.23.3206. PubMed: 9389652.
    • (1997) Genes Dev , vol.11 , pp. 3206-3217
    • Alspaugh, J.A.1    Perfect, J.R.2    Heitman, J.3
  • 64
    • 22844445893 scopus 로고    scopus 로고
    • Aspergillus fumigatus conidial pigment and cAMP signal transduction: significance for virulence
    • 10.1080/13693780400028967
    • Brakhage AA, Liebmann B, (2005) Aspergillus fumigatus conidial pigment and cAMP signal transduction: significance for virulence. Med Mycol 43 (Suppl 1):: S75-S82. doi:10.1080/13693780400028967. PubMed: 16110796.
    • (2005) Med Mycol , vol.43 , Issue.SUPPL. 1
    • Brakhage, A.A.1    Liebmann, B.2
  • 65
    • 0031742618 scopus 로고    scopus 로고
    • Control of pigmentation of Ustilago hordei: the effect of pH, thiamine, and involvement of the cAMP cascade
    • 10.1006/fgbi.1998.1087
    • Lichter A, Mills D, (1998) Control of pigmentation of Ustilago hordei: the effect of pH, thiamine, and involvement of the cAMP cascade. Fungal Genet Biol 25: 63-74. doi:10.1006/fgbi.1998.1087. PubMed: 9806807.
    • (1998) Fungal Genet Biol , vol.25 , pp. 63-74
    • Lichter, A.1    Mills, D.2
  • 66
    • 0029816544 scopus 로고    scopus 로고
    • Breaking and entering: host penetration by the fungal rice blast pathogen Magnaporthe grisea
    • 10.1146/annurev.micro.50.1.491
    • Howard RJ, Valent B, (1996) Breaking and entering: host penetration by the fungal rice blast pathogen Magnaporthe grisea. Annu Rev Microbiol 50: 491-512. doi:10.1146/annurev.micro.50.1.491. PubMed: 8905089.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 491-512
    • Howard, R.J.1    Valent, B.2
  • 67
    • 42549135491 scopus 로고    scopus 로고
    • Altered patterns of gene duplication and differential gene gain and loss in fungal pathogens
    • 10.1186/1471-2164-9-147
    • Powell AJ, Conant GC, Brown DE, Carbone I, Dean RA, (2008) Altered patterns of gene duplication and differential gene gain and loss in fungal pathogens. BMC Genomics 9: 147. doi:10.1186/1471-2164-9-147. PubMed: 18373860.
    • (2008) BMC Genomics , vol.9 , pp. 147
    • Powell, A.J.1    Conant, G.C.2    Brown, D.E.3    Carbone, I.4    Dean, R.A.5
  • 68
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • 10.1038/35054500
    • Peters C, Bayer MJ, Bühler S, Andersen JS, Mann M, et al. (2001) Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 409: 581-588. doi:10.1038/35054500. PubMed: 11214310.
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Bühler, S.3    Andersen, J.S.4    Mann, M.5
  • 69
    • 80054953356 scopus 로고    scopus 로고
    • The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles
    • 10.1038/emboj.2011.335
    • Strasser B, Iwaszkiewicz J, Michielin O, Mayer A, (2011) The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles. EMBO J 30: 4126-4141. doi:10.1038/emboj.2011.335. PubMed: 21934648.
    • (2011) EMBO J , vol.30 , pp. 4126-4141
    • Strasser, B.1    Iwaszkiewicz, J.2    Michielin, O.3    Mayer, A.4
  • 70
    • 79551516483 scopus 로고    scopus 로고
    • MoVam7, a conserved SNARE involved in vacuole assembly, is required for growth, endocytosis, ROS accumulation, and pathogenesis of Magnaporthe oryzae
    • 10.1371/journal.pone.0016439
    • Dou X, Wang Q, Qi Z, Song W, Wang W, et al. (2011) MoVam7, a conserved SNARE involved in vacuole assembly, is required for growth, endocytosis, ROS accumulation, and pathogenesis of Magnaporthe oryzae. PLOS ONE 6: e16439. doi:10.1371/journal.pone.0016439. PubMed: 21283626.
    • (2011) PLOS ONE , vol.6
    • Dou, X.1    Wang, Q.2    Qi, Z.3    Song, W.4    Wang, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.