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Volumn 1840, Issue 5, 2014, Pages 1482-1491

Yeast reveals unexpected roles and regulatory features of aquaporins and aquaglyceroporins

Author keywords

Aquaporin; Freeze tolerance; MAPK pathway; Osmoregulation; Signal transduction; Stress resistance

Indexed keywords

ACETIC ACID; AQUAGLYCEROPORIN; AQUAPORIN; AQUAPORIN 1; AQUAPORIN 2; GLYCEROL; MEMBRANE PROTEIN; METALLOID; PROTEIN FPS1; PROTEIN HOG1; UNCLASSIFIED DRUG;

EID: 84897114271     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.09.027     Document Type: Review
Times cited : (55)

References (92)
  • 1
    • 4444221676 scopus 로고    scopus 로고
    • From structure to disease: The evolving tale of aquaporin biology
    • DOI 10.1038/nrm1469
    • L.S. King, D. Kozono, and P. Agre From structure to disease: the evolving tale of aquaporin biology Nat. Rev. Mol. Cell Biol. 5 2004 687 698 (Pubitemid 39208179)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.9 , pp. 687-698
    • King, L.S.1    Kozono, D.2    Agre, P.3
  • 2
    • 84855932788 scopus 로고    scopus 로고
    • Aquaporins in clinical medicine
    • A.S. Verkman Aquaporins in clinical medicine Annu. Rev. Med. 63 2012 303 316
    • (2012) Annu. Rev. Med. , vol.63 , pp. 303-316
    • Verkman, A.S.1
  • 4
    • 44949265295 scopus 로고    scopus 로고
    • Plant aquaporins: Membrane channels with multiple integrated functions
    • DOI 10.1146/annurev.arplant.59.032607.092734
    • C. Maurel, L. Verdoucq, D.T. Luu, and V. Santoni Plant aquaporins: membrane channels with multiple integrated functions Annu. Rev. Plant Biol. 59 2008 595 624 (Pubitemid 351813044)
    • (2008) Annual Review of Plant Biology , vol.59 , pp. 595-624
    • Maure, C.1    Verdoucq, L.2    Luu, D.-T.3    Santoni, V.4
  • 5
    • 81255197643 scopus 로고    scopus 로고
    • Yeast: An experimental organism for 21st Century biology
    • D. Botstein, and G.R. Fink Yeast: an experimental organism for 21st Century biology Genetics 189 2011 695 704
    • (2011) Genetics , vol.189 , pp. 695-704
    • Botstein, D.1    Fink, G.R.2
  • 6
    • 77953754620 scopus 로고    scopus 로고
    • Yeast evolutionary genomics
    • B. Dujon Yeast evolutionary genomics Nat. Rev. Genet. 11 2010 512 524
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 512-524
    • Dujon, B.1
  • 7
    • 84860548726 scopus 로고    scopus 로고
    • Mating-type genes and MAT switching in Saccharomyces cerevisiae
    • J.E. Haber Mating-type genes and MAT switching in Saccharomyces cerevisiae Genetics 191 2012 33 64
    • (2012) Genetics , vol.191 , pp. 33-64
    • Haber, J.E.1
  • 8
    • 81255176779 scopus 로고    scopus 로고
    • Sporulation in the budding yeast Saccharomyces cerevisiae
    • A.M. Neiman Sporulation in the budding yeast Saccharomyces cerevisiae Genetics 189 2011 737 765
    • (2011) Genetics , vol.189 , pp. 737-765
    • Neiman, A.M.1
  • 9
    • 84867162776 scopus 로고    scopus 로고
    • Response to hyperosmotic stress
    • H. Saito, and F. Posas Response to hyperosmotic stress Genetics 192 2012 289 318
    • (2012) Genetics , vol.192 , pp. 289-318
    • Saito, H.1    Posas, F.2
  • 10
    • 71149097450 scopus 로고    scopus 로고
    • Control of high osmolarity signalling in the yeast Saccharomyces cerevisiae
    • S. Hohmann Control of high osmolarity signalling in the yeast Saccharomyces cerevisiae FEBS Lett. 583 2009 4025 4029
    • (2009) FEBS Lett. , vol.583 , pp. 4025-4029
    • Hohmann, S.1
  • 11
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • DOI 10.1128/MMBR.66.2.300-372.2002
    • S. Hohmann Osmotic stress signaling and osmoadaptation in yeasts Microbiol. Mol. Biol. Rev. 66 2002 300 372 (Pubitemid 34625712)
    • (2002) Microbiology and Molecular Biology Reviews , vol.66 , Issue.2 , pp. 300-372
    • Hohmann, S.1
  • 13
    • 83455179434 scopus 로고    scopus 로고
    • Regulation of cell wall biogenesis in Saccharomyces cerevisiae: The cell wall integrity signaling pathway
    • D.E. Levin Regulation of cell wall biogenesis in Saccharomyces cerevisiae: the cell wall integrity signaling pathway Genetics 189 2011 1145 1175
    • (2011) Genetics , vol.189 , pp. 1145-1175
    • Levin, D.E.1
  • 14
    • 34547216984 scopus 로고    scopus 로고
    • Function and regulation in MAPK signaling pathways: Lessons learned from the yeast Saccharomyces cerevisiae
    • DOI 10.1016/j.bbamcr.2007.05.003, PII S0167488907001218
    • R.E. Chen, and J. Thorner Function and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiae Biochim. Biophys. Acta 1773 2007 1311 1340 (Pubitemid 47125982)
    • (2007) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1773 , Issue.8 , pp. 1311-1340
    • Chen, R.E.1    Thorner, J.2
  • 15
    • 84876826813 scopus 로고    scopus 로고
    • Pheromone-induced morphogenesis improves osmoadaptation capacity by activating the HOG MAPK pathway
    • R. Baltanas, A. Bush, A. Couto, L. Durrieu, S. Hohmann, and A. Colman-Lerner Pheromone-induced morphogenesis improves osmoadaptation capacity by activating the HOG MAPK pathway Sci. Signal. 6 2013 ra26
    • (2013) Sci. Signal. , vol.6 , pp. 26
    • Baltanas, R.1    Bush, A.2    Couto, A.3    Durrieu, L.4    Hohmann, S.5    Colman-Lerner, A.6
  • 18
    • 77952332278 scopus 로고    scopus 로고
    • Incipient balancing selection through adaptive loss of aquaporins in natural Saccharomyces cerevisiae populations
    • J.L. Will, H.S. Kim, J. Clarke, J.C. Painter, J.C. Fay, and A.P. Gasch Incipient balancing selection through adaptive loss of aquaporins in natural Saccharomyces cerevisiae populations PLoS Genet. 6 2010 e1000893
    • (2010) PLoS Genet. , vol.6 , pp. 1000893
    • Will, J.L.1    Kim, H.S.2    Clarke, J.3    Painter, J.C.4    Fay, J.C.5    Gasch, A.P.6
  • 20
    • 0032538552 scopus 로고    scopus 로고
    • Aquaporins in Saccharomyces: Genetic and functional distinctions between laboratory and wild-type strains
    • DOI 10.1074/jbc.273.42.27565
    • M. Bonhivers, J.M. Carbrey, S.J. Gould, and P. Agre Aquaporins in Saccharomyces. Genetic and functional distinctions between laboratory and wild-type strains J. Biol. Chem. 273 1998 27565 27572 (Pubitemid 28500478)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27565-27572
    • Bonhivers, M.1    Carbrey, J.M.2    Gould, S.J.3    Agre, P.4
  • 21
    • 0033927503 scopus 로고    scopus 로고
    • Polymorphism of Saccharomyces cerevisiae aquaporins
    • DOI 10.1002/1097-0061(200007)16:10<897::AID-YEA583>3.0.CO;2-T
    • V. Laize, F. Tacnet, P. Ripoche, and S. Hohmann Polymorphism of Saccharomyces cerevisiae aquaporins Yeast 16 2000 897 903 (Pubitemid 30466096)
    • (2000) Yeast , vol.16 , Issue.10 , pp. 897-903
    • Laize, V.1    Tacnet, F.2    Ripoche, P.3    Hohmann, S.4
  • 22
  • 24
    • 33645006905 scopus 로고    scopus 로고
    • Aquaporins in Saccharomyces cerevisiae wine yeast
    • J.E. Karpel, and L.F. Bisson Aquaporins in Saccharomyces cerevisiae wine yeast FEMS Microbiol. Lett. 257 2006 117 123
    • (2006) FEMS Microbiol. Lett. , vol.257 , pp. 117-123
    • Karpel, J.E.1    Bisson, L.F.2
  • 25
    • 0035187226 scopus 로고    scopus 로고
    • Aquaporin in Candida: Characterization of a functional water channel protein
    • J.M. Carbrey, B.P. Cormack, and P. Agre Aquaporin in Candida: characterization of a functional water channel protein Yeast 18 2001 1391 1396
    • (2001) Yeast , vol.18 , pp. 1391-1396
    • Carbrey, J.M.1    Cormack, B.P.2    Agre, P.3
  • 26
    • 0036952087 scopus 로고    scopus 로고
    • Aquaporin expression correlates with freeze tolerance in baker's yeast, and overexpression improves freeze tolerance in industrial strains
    • DOI 10.1128/AEM.68.12.5981-5989.2002
    • A. Tanghe, P. Van Dijck, F. Dumortier, A. Teunissen, S. Hohmann, and J.M. Thevelein Aquaporin expression correlates with freeze tolerance in baker's yeast, and overexpression improves freeze tolerance in industrial strains Appl. Environ. Microbiol. 68 2002 5981 5989 (Pubitemid 36342431)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.12 , pp. 5981-5989
    • Tanghe, A.1    Van Dijck, P.2    Dumortier, F.3    Teunissen, A.4    Hohmann, S.5    Thevelein, J.M.6
  • 30
    • 2942593752 scopus 로고    scopus 로고
    • Aquaporin-mediated improvement of freeze tolerance of saccharomyces cerevisiae is restricted to rapid freezing conditions
    • DOI 10.1128/AEM.70.6.3377-3382.2004
    • A. Tanghe, P. Van Dijck, D. Colavizza, and J.M. Thevelein Aquaporin-mediated improvement of freeze tolerance of Saccharomyces cerevisiae is restricted to rapid freezing conditions Appl. Environ. Microbiol. 70 2004 3377 3382 (Pubitemid 38745881)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.6 , pp. 3377-3382
    • Tanghe, A.1    Van Dijck, P.2    Colavizza, D.3    Thevelein, J.M.4
  • 31
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • G.M. Preston, T.P. Carroll, W.B. Guggino, and P. Agre Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein Science 256 1992 385 387
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 32
    • 33646832951 scopus 로고    scopus 로고
    • Water channels are important for osmotic adjustments of yeast cells at low temperature
    • DOI 10.1099/mic.0.28679-0
    • G. Soveral, A. Veiga, M.C. Loureiro-Dias, A. Tanghe, P. Van Dijck, and T.F. Moura Water channels are important for osmotic adjustments of yeast cells at low temperature Microbiology 152 2006 1515 1521 (Pubitemid 43772038)
    • (2006) Microbiology , vol.152 , Issue.5 , pp. 1515-1521
    • Soveral, G.1    Veiga, A.2    Loureiro-Dias, M.C.3    Tanghe, A.4    Van Dijck, P.5    Moura, T.F.6
  • 35
    • 70450217298 scopus 로고    scopus 로고
    • Expression of the yeast aquaporin Aqy2 affects cell surface properties under the control of osmoregulatory and morphogenic signalling pathways
    • K. Furukawa, F. Sidoux-Walter, and S. Hohmann Expression of the yeast aquaporin Aqy2 affects cell surface properties under the control of osmoregulatory and morphogenic signalling pathways Mol. Microbiol. 74 2009 1272 1286
    • (2009) Mol. Microbiol. , vol.74 , pp. 1272-1286
    • Furukawa, K.1    Sidoux-Walter, F.2    Hohmann, S.3
  • 36
    • 84855445916 scopus 로고    scopus 로고
    • The regulation of filamentous growth in yeast
    • P.J. Cullen, and G.F. Sprague Jr. The regulation of filamentous growth in yeast Genetics 190 2012 23 49
    • (2012) Genetics , vol.190 , pp. 23-49
    • Cullen, P.J.1    Sprague, Jr.G.F.2
  • 37
    • 78449252869 scopus 로고    scopus 로고
    • General factors important for the formation of structured biofilm-like yeast colonies
    • V. St'ovicek, L. Vachova, M. Kuthan, and Z. Palkova General factors important for the formation of structured biofilm-like yeast colonies Fungal Genet. Biol. 47 2010 1012 1022
    • (2010) Fungal Genet. Biol. , vol.47 , pp. 1012-1022
    • St'Ovicek, V.1    Vachova, L.2    Kuthan, M.3    Palkova, Z.4
  • 38
    • 0037238176 scopus 로고    scopus 로고
    • Domestication of wild Saccharomyces cerevisiae is accompanied by changes in gene expression and colony morphology
    • DOI 10.1046/j.1365-2958.2003.03332.x
    • M. Kuthan, F. Devaux, B. Janderova, I. Slaninova, C. Jacq, and Z. Palkova Domestication of wild Saccharomyces cerevisiae is accompanied by changes in gene expression and colony morphology Mol. Microbiol. 47 2003 745 754 (Pubitemid 36114982)
    • (2003) Molecular Microbiology , vol.47 , Issue.3 , pp. 745-754
    • Kuthan, M.1    Devaux, F.2    Janderova, B.3    Slaninova, I.4    Jacq, C.5    Palkova, Z.6
  • 39
    • 33746865230 scopus 로고    scopus 로고
    • Life within a community: Benefit to yeast long-term survival
    • DOI 10.1111/j.1574-6976.2006.00034.x
    • Z. Palkova, and L. Vachova Life within a community: benefit to yeast long-term survival FEMS Microbiol. Rev. 30 2006 806 824 (Pubitemid 44199351)
    • (2006) FEMS Microbiology Reviews , vol.30 , Issue.5 , pp. 806-824
    • Palkova, Z.1    Vachova, L.2
  • 40
    • 84887530043 scopus 로고    scopus 로고
    • Further advances in the production of membrane proteins in Pichia pastoris
    • K. Hedfalk Further advances in the production of membrane proteins in Pichia pastoris Bioengineered 4 2013
    • (2013) Bioengineered , vol.4
    • Hedfalk, K.1
  • 44
    • 84878928639 scopus 로고    scopus 로고
    • Recombinant production of the human aquaporins in the yeast Pichia pastoris
    • F. Oberg, and K. Hedfalk Recombinant production of the human aquaporins in the yeast Pichia pastoris Mol. Membr. Biol. 30 2013 15 31
    • (2013) Mol. Membr. Biol. , vol.30 , pp. 15-31
    • Oberg, F.1    Hedfalk, K.2
  • 45
    • 0034933591 scopus 로고    scopus 로고
    • The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae
    • DOI 10.1046/j.1365-2958.2001.02485.x
    • R. Wysocki, C.C. Chery, D. Wawrzycka, M. Van Hulle, R. Cornelis, J.M. Thevelein, and M.J. Tamas The glycerol channel Fps1p mediates the uptake of arsenite and antimonite in Saccharomyces cerevisiae Mol. Microbiol. 40 2001 1391 1401 (Pubitemid 32635307)
    • (2001) Molecular Microbiology , vol.40 , Issue.6 , pp. 1391-1401
    • Wysocki, R.1    Chery, C.C.2    Wawrzycka, D.3    Van Hulle, M.4    Cornelis, R.5    Thevelein, J.M.6    Tamas, M.J.7
  • 47
    • 33747697862 scopus 로고    scopus 로고
    • Roles of BOR1, DUR3, and FPS1 in boron transport and tolerance in Saccharomyces cerevisiae
    • DOI 10.1111/j.1574-6968.2006.00395.x
    • A. Nozawa, J. Takano, M. Kobayashi, N. von Wiren, and T. Fujiwara Roles of BOR1, DUR3, and FPS1 in boron transport and tolerance in Saccharomyces cerevisiae FEMS Microbiol. Lett. 262 2006 216 222 (Pubitemid 44272798)
    • (2006) FEMS Microbiology Letters , vol.262 , Issue.2 , pp. 216-222
    • Nozawa, A.1    Takano, J.2    Kobayashi, M.3    Von Wiren, N.4    Fujiwara, T.5
  • 48
    • 77954496148 scopus 로고    scopus 로고
    • The Fps1p aquaglyceroporin facilitates the use of small aliphatic amides as a nitrogen source by amidase-expressing yeasts
    • A. Shepherd, and P.W. Piper The Fps1p aquaglyceroporin facilitates the use of small aliphatic amides as a nitrogen source by amidase-expressing yeasts FEMS Yeast Res. 10 2010 527 534
    • (2010) FEMS Yeast Res. , vol.10 , pp. 527-534
    • Shepherd, A.1    Piper, P.W.2
  • 49
    • 83055196833 scopus 로고    scopus 로고
    • Yeast Fps1 glycerol facilitator functions as a homotetramer
    • S.E. Beese-Sims, J. Lee, and D.E. Levin Yeast Fps1 glycerol facilitator functions as a homotetramer Yeast 28 2011 815 819
    • (2011) Yeast , vol.28 , pp. 815-819
    • Beese-Sims, S.E.1    Lee, J.2    Levin, D.E.3
  • 51
    • 0037805604 scopus 로고    scopus 로고
    • Fps1p channel is the mediator of the major part of glycerol passive diffusion in Saccharomyces cerevisiae: Artefacts and re-definitions
    • DOI 10.1016/S0005-2736(03)00138-X
    • R. Oliveira, F. Lages, M. Silva-Graca, and C. Lucas Fps1p channel is the mediator of the major part of glycerol passive diffusion in Saccharomyces cerevisiae: artefacts and re-definitions Biochim. Biophys. Acta 1613 2003 57 71 (Pubitemid 36780955)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1613 , Issue.1-2 , pp. 57-71
    • Oliveira, R.1    Lages, F.2    Silva-Graca, M.3    Lucas, C.4
  • 53
    • 0025772978 scopus 로고
    • A yeast homologue of the bovine lens fibre MIP gene family complements the growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars but not its defect in glucose-induced RAS-mediated cAMP signalling
    • L. Van Aelst, S. Hohmann, F.K. Zimmermann, A.W. Jans, and J.M. Thevelein A yeast homologue of the bovine lens fibre MIP gene family complements the growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars but not its defect in glucose-induced RAS-mediated cAMP signalling EMBO J. 10 1991 2095 2104 (Pubitemid 21905681)
    • (1991) EMBO Journal , vol.10 , Issue.8 , pp. 2095-2104
    • Van Aelst, L.1    Hohmann, S.2    Zimmermann, F.K.3    Jans, A.W.H.4    Thevelein, J.M.5
  • 55
    • 0028985536 scopus 로고
    • Trehalose synthase: Guard to the gate of glycolysis in yeast?
    • J.M. Thevelein, and S. Hohmann Trehalose synthase: guard to the gate of glycolysis in yeast? Trends Biochem. Sci. 20 1995 3 10
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 3-10
    • Thevelein, J.M.1    Hohmann, S.2
  • 56
    • 0027534678 scopus 로고
    • The growth and signalling defects of the ggs1 (fdp1/byp1) deletion mutant on glucose are suppressed by a deletion of the gene encoding hexokinase PII
    • S. Hohmann, M.J. Neves, W. de Koning, R. Alijo, J. Ramos, and J.M. Thevelein The growth and signalling defects of the ggs1 (fdp1/byp1) deletion mutant on glucose are suppressed by a deletion of the gene encoding hexokinase PII Curr. Genet. 23 1993 281 289 (Pubitemid 23096104)
    • (1993) Current Genetics , vol.23 , Issue.4 , pp. 281-289
    • Hohmann, S.1    Neves, M.J.2    De Koning, W.3    Alijo, R.4    Ramos, J.5    Thevelein, J.M.6
  • 57
    • 0028947362 scopus 로고
    • Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress
    • K. Luyten, J. Albertyn, W.F. Skibbe, B.A. Prior, J. Ramos, J.M. Thevelein, and S. Hohmann Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress EMBO J. 14 1995 1360 1371
    • (1995) EMBO J. , vol.14 , pp. 1360-1371
    • Luyten, K.1    Albertyn, J.2    Skibbe, W.F.3    Prior, B.A.4    Ramos, J.5    Thevelein, J.M.6    Hohmann, S.7
  • 58
    • 0014305533 scopus 로고
    • Glycerol metabolism in yeasts. Pathways of utilization and production
    • C. Gancedo, J.M. Gancedo, and A. Sols Glycerol metabolism in yeasts. Pathways of utilization and production Eur. J. Biochem. 5 1968 165 172
    • (1968) Eur. J. Biochem. , vol.5 , pp. 165-172
    • Gancedo, C.1    Gancedo, J.M.2    Sols, A.3
  • 60
    • 78049331320 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae glycerol/H + symporter Stl1p is essential for cold/near-freeze and freeze stress adaptation. A simple recipe with high biotechnological potential is given
    • J. Tulha, A. Lima, C. Lucas, and C. Ferreira Saccharomyces cerevisiae glycerol/H + symporter Stl1p is essential for cold/near-freeze and freeze stress adaptation. A simple recipe with high biotechnological potential is given Microb. Cell Fact. 9 2010 82
    • (2010) Microb. Cell Fact. , vol.9 , pp. 82
    • Tulha, J.1    Lima, A.2    Lucas, C.3    Ferreira, C.4
  • 61
    • 0034708436 scopus 로고    scopus 로고
    • The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathway-dependent genes
    • DOI 10.1074/jbc.275.12.8290
    • M. Rep, M. Krantz, J.M. Thevelein, and S. Hohmann The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathway-dependent genes J. Biol. Chem. 275 2000 8290 8300 (Pubitemid 30180168)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.12 , pp. 8290-8300
    • Rep, M.1    Krantz, M.2    Thevelein, J.M.3    Hohmann, S.4
  • 65
    • 73649121261 scopus 로고    scopus 로고
    • Identification of positive regulators of the yeast fps1 glycerol channel
    • S.E. Beese, T. Negishi, and D.E. Levin Identification of positive regulators of the yeast fps1 glycerol channel PLoS Genet. 5 2009 e1000738
    • (2009) PLoS Genet. , vol.5 , pp. 1000738
    • Beese, S.E.1    Negishi, T.2    Levin, D.E.3
  • 66
    • 0242475404 scopus 로고    scopus 로고
    • Physiological response to anaerobicity of glycerol-3-phosphate dehydrogenase mutants of Saccharomyces cerevisiae
    • S. Bjorkqvist, R. Ansell, L. Adler, and G. Liden Physiological response to anaerobicity of glycerol-3-phosphate dehydrogenase mutants of Saccharomyces cerevisiae Appl. Environ. Microbiol. 63 1997 128 132 (Pubitemid 27020379)
    • (1997) Applied and Environmental Microbiology , vol.63 , Issue.1 , pp. 128-132
    • Bjorkqvist, S.1    Ansell, R.2    Adler, L.3    Liden, G.4
  • 67
    • 0030908893 scopus 로고    scopus 로고
    • +-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation
    • DOI 10.1093/emboj/16.9.2179
    • R. Ansell, K. Granath, S. Hohmann, J.M. Thevelein, and L. Adler The two isoenzymes for yeast NAD + - dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation EMBO J. 16 1997 2179 2187 (Pubitemid 27258621)
    • (1997) EMBO Journal , vol.16 , Issue.9 , pp. 2179-2187
    • Ansell, R.1    Granath, K.2    Hohmann, S.3    Thevelein, J.M.4    Adler, L.5
  • 68
    • 0029786406 scopus 로고    scopus 로고
    • Influence of the nitrogen source on Saccharomyces cerevisiae anaerobic growth and product formation
    • E. Albers, C. Larsson, G. Liden, C. Niklasson, and L. Gustafsson Influence of the nitrogen source on Saccharomyces cerevisiae anaerobic growth and product formation Appl. Environ. Microbiol. 62 1996 3187 3195 (Pubitemid 26304100)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.9 , pp. 3187-3195
    • Albers, E.1    Larsson, C.2    Liden, G.3    Niklasson, C.4    Gustafsson, L.5
  • 69
    • 0030884717 scopus 로고    scopus 로고
    • Osmotic balance regulates cell fusion during mating in Saccharomyces cerevisiae
    • DOI 10.1083/jcb.138.5.961
    • J. Philips, and I. Herskowitz Osmotic balance regulates cell fusion during mating in Saccharomyces cerevisiae J. Cell Biol. 138 1997 961 974 (Pubitemid 27386448)
    • (1997) Journal of Cell Biology , vol.138 , Issue.5 , pp. 961-974
    • Philips, J.1    Herskowitz, I.2
  • 70
    • 0035733930 scopus 로고    scopus 로고
    • Implications of FPS1 deletion and membrane ergosterol content for glycerol efflux from Saccharomyces cerevisiae
    • DOI 10.1016/S1567-1356(01)00032-0, PII S1567135601000320
    • T.H. Toh, G. Kayingo, M.J. van der Merwe, S.G. Kilian, J.E. Hallsworth, S. Hohmann, and B.A. Prior Implications of FPS1 deletion and membrane ergosterol content for glycerol efflux from Saccharomyces cerevisiae FEMS Yeast Res. 1 2001 205 211 (Pubitemid 34442269)
    • (2001) FEMS Yeast Research , vol.1 , Issue.3 , pp. 205-211
    • Toh, T.-H.1    Kayingo, G.2    Van Der Merwe, M.J.3    Kilian, S.G.4    Hallsworth, J.E.5    Hohmann, S.6    Prior, B.A.7
  • 71
    • 0033923859 scopus 로고    scopus 로고
    • The control of intracellular glycerol in Saccharomyces cerevisiae influences osmotic stress response and resistance to increased temperature
    • DOI 10.1046/j.1365-2958.2000.01955.x
    • M. Siderius, O. Van Wuytswinkel, K.A. Reijenga, M. Kelders, and W.H. Mager The control of intracellular glycerol in Saccharomyces cerevisiae influences osmotic stress response and resistance to increased temperature Mol. Microbiol. 36 2000 1381 1390 (Pubitemid 30449973)
    • (2000) Molecular Microbiology , vol.36 , Issue.6 , pp. 1381-1390
    • Siderius, M.1    Van Wuytswinkel, O.2    Reijenga, K.A.3    Kelders, M.4    Mager, W.H.5
  • 72
    • 7044282883 scopus 로고    scopus 로고
    • Intracellular glycerol influences resistance to freeze stress in Saccharomyces cerevisiae: Analysis of a quadruple mutant in glycerol dehydrogenase genes and glycerol-enriched cells
    • S. Izawa, M. Sato, K. Yokoigawa, and Y. Inoue Intracellular glycerol influences resistance to freeze stress in Saccharomyces cerevisiae: analysis of a quadruple mutant in glycerol dehydrogenase genes and glycerol-enriched cells Appl. Microbiol. Biotechnol. 66 2004 108 114
    • (2004) Appl. Microbiol. Biotechnol. , vol.66 , pp. 108-114
    • Izawa, S.1    Sato, M.2    Yokoigawa, K.3    Inoue, Y.4
  • 73
    • 11244306063 scopus 로고    scopus 로고
    • Deficiency in the glycerol channel Fps1p confers increased freeze tolerance to yeast cells: Application of the fps1Δ mutant to frozen dough technology
    • DOI 10.1007/s00253-004-1688-1
    • S. Izawa, K. Ikeda, K. Maeta, and Y. Inoue Deficiency in the glycerol channel Fps1p confers increased freeze tolerance to yeast cells: application of the fps1delta mutant to frozen dough technology Appl. Microbiol. Biotechnol. 66 2004 303 305 (Pubitemid 40064361)
    • (2004) Applied Microbiology and Biotechnology , vol.66 , Issue.3 , pp. 303-305
    • Izawa, S.1    Ikeda, K.2    Maeta, K.3    Inoue, Y.4
  • 75
    • 48749096008 scopus 로고    scopus 로고
    • Carcinogenic metal compounds: Recent insight into molecular and cellular mechanisms
    • D. Beyersmann, and A. Hartwig Carcinogenic metal compounds: recent insight into molecular and cellular mechanisms Arch. Toxicol. 82 2008 493 512
    • (2008) Arch. Toxicol. , vol.82 , pp. 493-512
    • Beyersmann, D.1    Hartwig, A.2
  • 76
    • 0037150531 scopus 로고    scopus 로고
    • Public health. Worldwide occurrences of arsenic in ground water
    • D.K. Nordstrom Public health. Worldwide occurrences of arsenic in ground water Science 296 2002 2143 2145
    • (2002) Science , vol.296 , pp. 2143-2145
    • Nordstrom, D.K.1
  • 77
    • 68649102607 scopus 로고    scopus 로고
    • Pentavalent antimonials: New perspectives for old drugs
    • F. Frezard, C. Demicheli, and R.R. Ribeiro Pentavalent antimonials: new perspectives for old drugs Molecules 14 2009 2317 2336
    • (2009) Molecules , vol.14 , pp. 2317-2336
    • Frezard, F.1    Demicheli, C.2    Ribeiro, R.R.3
  • 78
    • 34548434715 scopus 로고    scopus 로고
    • Arsenical-based cancer drugs
    • DOI 10.1016/j.ctrv.2007.05.001, PII S0305737207000734
    • P.J. Dilda, and P.J. Hogg Arsenical-based cancer drugs Cancer Treat. Rev. 33 2007 542 564 (Pubitemid 47355338)
    • (2007) Cancer Treatment Reviews , vol.33 , Issue.6 , pp. 542-564
    • Dilda, P.J.1    Hogg, P.J.2
  • 79
    • 42749092894 scopus 로고    scopus 로고
    • The Arabidopsis thaliana aquaglyceroporin AtNIP7;1 is a pathway for arsenite uptake
    • S.V. Isayenkov, and F.J. Maathuis The Arabidopsis thaliana aquaglyceroporin AtNIP7;1 is a pathway for arsenite uptake FEBS Lett. 582 2008 1625 1628
    • (2008) FEBS Lett. , vol.582 , pp. 1625-1628
    • Isayenkov, S.V.1    Maathuis, F.J.2
  • 80
    • 47349127025 scopus 로고    scopus 로고
    • A subgroup of plant aquaporins facilitate the bi-directional diffusion of As(OH)3 and Sb(OH)3 across membranes
    • G.P. Bienert, M. Thorsen, M.D. Schussler, H.R. Nilsson, A. Wagner, M.J. Tamas, and T.P. Jahn A subgroup of plant aquaporins facilitate the bi-directional diffusion of As(OH)3 and Sb(OH)3 across membranes BMC Biol. 6 2008 26
    • (2008) BMC Biol. , vol.6 , pp. 26
    • Bienert, G.P.1    Thorsen, M.2    Schussler, M.D.3    Nilsson, H.R.4    Wagner, A.5    Tamas, M.J.6    Jahn, T.P.7
  • 82
    • 11144354454 scopus 로고    scopus 로고
    • Experimental and theoretical characterization of arsenite in water: Insights into the coordination environment of As-O
    • A. Ramirez-Solis, R. Mukopadhyay, B.P. Rosen, and T.L. Stemmler Experimental and theoretical characterization of arsenite in water: insights into the coordination environment of As-O Inorg. Chem. 43 2004 2954 2959
    • (2004) Inorg. Chem. , vol.43 , pp. 2954-2959
    • Ramirez-Solis, A.1    Mukopadhyay, R.2    Rosen, B.P.3    Stemmler, T.L.4
  • 83
    • 0030953720 scopus 로고    scopus 로고
    • Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli
    • O.I. Sanders, C. Rensing, M. Kuroda, B. Mitra, and B.P. Rosen Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli J. Bacteriol. 179 1997 3365 3367 (Pubitemid 27203017)
    • (1997) Journal of Bacteriology , vol.179 , Issue.10 , pp. 3365-3367
    • Sanders, O.I.1    Rensing, C.2    Kuroda, M.3    Mitra, B.4    Rosen, B.P.5
  • 84
    • 35148901172 scopus 로고    scopus 로고
    • 3 with glycerol: Implications for their uptake
    • DOI 10.1021/tx700110m
    • A. Porquet, and M. Filella Structural evidence of the similarity of Sb(OH)3 and As(OH)3 with glycerol: implications for their uptake Chem. Res. Toxicol. 20 2007 1269 1276 (Pubitemid 47548295)
    • (2007) Chemical Research in Toxicology , vol.20 , Issue.9 , pp. 1269-1276
    • Porquet, A.1    Filella, M.2
  • 85
    • 79954414844 scopus 로고    scopus 로고
    • A genome-wide perspective on the response and tolerance to food-relevant stresses in Saccharomyces cerevisiae
    • M.C. Teixeira, N.P. Mira, and I. Sa-Correia A genome-wide perspective on the response and tolerance to food-relevant stresses in Saccharomyces cerevisiae Curr. Opin. Biotechnol. 22 2011 150 156
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 150-156
    • Teixeira, M.C.1    Mira, N.P.2    Sa-Correia, I.3
  • 86
    • 34548775911 scopus 로고    scopus 로고
    • Hog1 mitogen-activated protein kinase phosphorylation targets the yeast Fps1 aquaglyceroporin for endocytosis, thereby rendering cells resistant to acetic acid
    • DOI 10.1128/MCB.02205-06
    • M. Mollapour, and P.W. Piper Hog1 mitogen-activated protein kinase phosphorylation targets the yeast Fps1 aquaglyceroporin for endocytosis, thereby rendering cells resistant to acetic acid Mol. Cell. Biol. 27 2007 6446 6456 (Pubitemid 47435750)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.18 , pp. 6446-6456
    • Mollapour, M.1    Piper, P.W.2
  • 89
    • 1342322689 scopus 로고    scopus 로고
    • Identification of residues controlling transport through the yeast aquaglyceroporin Fps1 using a genetic screen
    • DOI 10.1111/j.1432-1033.2004.03980.x
    • S. Karlgren, C. Filipsson, J.G. Mullins, R.M. Bill, M.J. Tamas, and S. Hohmann Identification of residues controlling transport through the yeast aquaglyceroporin Fps1 using a genetic screen Eur. J. Biochem. 271 2004 771 779 (Pubitemid 38250920)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.4 , pp. 771-779
    • Karlgren, S.1    Filipsson, C.2    Mullins, J.G.L.3    Bill, R.M.4    Tamas, M.J.5    Hohmann, S.6
  • 92
    • 0029561101 scopus 로고
    • A second osmosensing signal transduction pathway in yeast. Hypotonic shock activates the PKC1 protein kinase-regulated cell integrity pathway
    • K.R. Davenport, M. Sohaskey, Y. Kamada, D.E. Levin, and M.C. Gustin A second osmosensing signal transduction pathway in yeast. Hypotonic shock activates the PKC1 protein kinase-regulated cell integrity pathway J. Biol. Chem. 270 1995 30157 30161
    • (1995) J. Biol. Chem. , vol.270 , pp. 30157-30161
    • Davenport, K.R.1    Sohaskey, M.2    Kamada, Y.3    Levin, D.E.4    Gustin, M.C.5


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