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Volumn 290, Issue 32, 2015, Pages 19874-19887

Yeast Fex1p is a constitutively expressed fluoride channel with functional asymmetry of its two homologous domains

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CYTOLOGY; IONS; PROTEINS; YEAST;

EID: 84939179305     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.651976     Document Type: Article
Times cited : (30)

References (60)
  • 2
    • 84859700950 scopus 로고    scopus 로고
    • Fluoride in drinking water and defluoridation of water
    • Jagtap, S., Yenkie, M. K., Labhsetwar, N., and Rayalu, S. (2012) Fluoride in drinking water and defluoridation of water. Chem. Rev. 112, 2454-2466
    • (2012) Chem. Rev. , vol.112 , pp. 2454-2466
    • Jagtap, S.1    Yenkie, M.K.2    Labhsetwar, N.3    Rayalu, S.4
  • 5
    • 0021704241 scopus 로고
    • Fluorine and Fluorides
    • IPCS International Programme on Chemical Safety, World Health Organization, Geneva
    • World Health Organization (1984) Fluorine and Fluorides, Environmental Health Criteria 36, IPCS International Programme on Chemical Safety, World Health Organization, Geneva
    • (1984) Environmental Health Criteria , vol.36
    • World Health Organization1
  • 10
    • 0027229920 scopus 로고
    • Fluoride inhibition of yeast enolase: Crystal structure of the enolase-Mg2+-F--Pi complex at 2.6 A resolution
    • Lebioda, L., Zhang, E., Lewinski, K., and Brewer, J. M. (1993) Fluoride inhibition of yeast enolase: crystal structure of the enolase-Mg2+-F--Pi complex at 2.6 A resolution. Proteins 16, 219-225
    • (1993) Proteins , vol.16 , pp. 219-225
    • Lebioda, L.1    Zhang, E.2    Lewinski, K.3    Brewer, J.M.4
  • 11
    • 84878400307 scopus 로고    scopus 로고
    • Molecular mechanisms of cytotoxicity and apoptosis induced by inorganic fluoride
    • Agalakova, N. I., and Gusev, G. P. (2012) Molecular mechanisms of cytotoxicity and apoptosis induced by inorganic fluoride. ISRN Cell Biol. 2012, 1-16
    • (2012) ISRN Cell Biol. , vol.2012 , pp. 1-16
    • Agalakova, N.I.1    Gusev, G.P.2
  • 12
    • 0037672768 scopus 로고    scopus 로고
    • The biochemistry and physiology of metallic fluoride: Action, mechanism, and implications
    • Li, L. (2003) The biochemistry and physiology of metallic fluoride: action, mechanism, and implications. Crit. Rev. Oral Biol. Med. 14, 100-114
    • (2003) Crit. Rev. Oral Biol. Med. , vol.14 , pp. 100-114
    • Li, L.1
  • 13
    • 33646853517 scopus 로고    scopus 로고
    • In vitro and in vivo effects of fluoride ions on enzyme activity
    • Adamek, E., Pawłowska-Góral, K., and Bober, K. (2005) In vitro and in vivo effects of fluoride ions on enzyme activity. Ann. Acad. Med. Stetin. 51, 69-85
    • (2005) Ann. Acad. Med. Stetin. , vol.51 , pp. 69-85
    • Adamek, E.1    Pawłowska-Góral, K.2    Bober, K.3
  • 15
    • 84883322489 scopus 로고    scopus 로고
    • A family of fluoride-specific ion channels with dual-topology architecture
    • Stockbridge, R. B., Robertson, J. L., Kolmakova-Partensky, L., and Miller, C. (2013) A family of fluoride-specific ion channels with dual-topology architecture. eLife 2, e01084
    • (2013) eLife , vol.2
    • Stockbridge, R.B.1    Robertson, J.L.2    Kolmakova-Partensky, L.3    Miller, C.4
  • 16
    • 84888090803 scopus 로고    scopus 로고
    • Eukaryotic resistance to fluoride toxicity mediated by a widespread family of fluoride export proteins
    • Li, S., Smith, K. D., Davis, J. H., Gordon, P. B., Breaker, R. R., and Strobel, S. A. (2013) Eukaryotic resistance to fluoride toxicity mediated by a widespread family of fluoride export proteins. Proc. Natl. Acad. Sci. U.S.A. 110, 19018-19023
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 19018-19023
    • Li, S.1    Smith, K.D.2    Davis, J.H.3    Gordon, P.B.4    Breaker, R.R.5    Strobel, S.A.6
  • 17
    • 84923322705 scopus 로고    scopus 로고
    • Proof of dual-topology architecture of Fluc F- channels with monobody blockers
    • Stockbridge, R. B., Koide, A., Miller, C., and Koide, S. (2014) Proof of dual-topology architecture of Fluc F- channels with monobody blockers. Nat. Commun. 5, 5120
    • (2014) Nat. Commun. , vol.5 , pp. 5120
    • Stockbridge, R.B.1    Koide, A.2    Miller, C.3    Koide, S.4
  • 20
    • 77957803530 scopus 로고    scopus 로고
    • How Saccharomyces cerevisiae copes with toxic metals and metalloids
    • Wysocki, R., and Tamás, M. J. (2010) How Saccharomyces cerevisiae copes with toxic metals and metalloids. FEMS Microbiol. Rev. 34, 925-951
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 925-951
    • Wysocki, R.1    Tamás, M.J.2
  • 21
    • 0030447223 scopus 로고    scopus 로고
    • Amino acid substitutions in membrane-spanning domains of Hol1, a member of the major facilitator superfamily of transporters, confer nonselective cation uptake in Saccharomyces cerevisiae
    • Wright, M. B., Howell, E. A., and Gaber, R. F. (1996) Amino acid substitutions in membrane-spanning domains of Hol1, a member of the major facilitator superfamily of transporters, confer nonselective cation uptake in Saccharomyces cerevisiae. J. Bacteriol. 178, 7197-7205
    • (1996) J. Bacteriol. , vol.178 , pp. 7197-7205
    • Wright, M.B.1    Howell, E.A.2    Gaber, R.F.3
  • 22
    • 84904346383 scopus 로고    scopus 로고
    • MFS transporters required for multidrug/multixenobiotic (MD/MX) resistance in the model yeast: Understanding their physiological function through post-genomic approaches
    • Dos Santos, S. C., Teixeira, M. C., Dias, P. J., and Sá-Correia, I. (2014) MFS transporters required for multidrug/multixenobiotic (MD/MX) resistance in the model yeast: understanding their physiological function through post-genomic approaches. Front. Physiol. 5, 180
    • (2014) Front. Physiol. , vol.5 , pp. 180
    • Dos Santos, S.C.1    Teixeira, M.C.2    Dias, P.J.3    Sá-Correia, I.4
  • 23
    • 33847697804 scopus 로고    scopus 로고
    • A cadmium-transporting P1B-type ATPase in yeast Saccharomyces cerevisiae
    • Adle, D. J., Sinani, D., Kim, H., and Lee, J. (2007) A cadmium-transporting P1B-type ATPase in yeast Saccharomyces cerevisiae. J. Biol. Chem. 282, 947-955
    • (2007) J. Biol. Chem. , vol.282 , pp. 947-955
    • Adle, D.J.1    Sinani, D.2    Kim, H.3    Lee, J.4
  • 24
    • 57649114599 scopus 로고    scopus 로고
    • Expressional control of a cadmium-transporting P1B-type ATPase by a metal sensing degradation signal
    • Adle, D. J., and Lee, J. (2008) Expressional control of a cadmium-transporting P1B-type ATPase by a metal sensing degradation signal. J. Biol. Chem. 283, 31460-31468
    • (2008) J. Biol. Chem. , vol.283 , pp. 31460-31468
    • Adle, D.J.1    Lee, J.2
  • 25
    • 67649854416 scopus 로고    scopus 로고
    • Cadmium-mediated rescue from ER-associated degradation induces expression of its exporter
    • Adle, D. J., Wei, W., Smith, N., Bies, J. J., and Lee, J. (2009) Cadmium-mediated rescue from ER-associated degradation induces expression of its exporter. Proc. Natl. Acad. Sci. U.S.A. 106, 10189-10194
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 10189-10194
    • Adle, D.J.1    Wei, W.2    Smith, N.3    Bies, J.J.4    Lee, J.5
  • 26
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman, F. (2002) Getting started with yeast. Methods Enzymol. 350, 3-41
    • (2002) Methods Enzymol. , vol.350 , pp. 3-41
    • Sherman, F.1
  • 28
    • 0031734798 scopus 로고    scopus 로고
    • Electrophysiology in the eukaryotic model cell Saccharomyces cerevisiae
    • Bertl, A., Bihler, H., Kettner, C., and Slayman, C. L. (1998) Electrophysiology in the eukaryotic model cell Saccharomyces cerevisiae. Pflugers Arch. 436, 999-1013
    • (1998) Pflugers Arch. , vol.436 , pp. 999-1013
    • Bertl, A.1    Bihler, H.2    Kettner, C.3    Slayman, C.L.4
  • 29
    • 2642571181 scopus 로고    scopus 로고
    • Chloride channel function in the yeast TRK-potassium transporters
    • Kuroda, T., Bihler, H., Bashi, E., Slayman, C. L., and Rivetta, A. (2004) Chloride channel function in the yeast TRK-potassium transporters. J. Membr. Biol. 198, 177-192
    • (2004) J. Membr. Biol. , vol.198 , pp. 177-192
    • Kuroda, T.1    Bihler, H.2    Bashi, E.3    Slayman, C.L.4    Rivetta, A.5
  • 30
    • 0027097849 scopus 로고
    • The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • Antebi, A., and Fink, G. R. (1992) The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 3, 633-654
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 31
    • 0033043209 scopus 로고    scopus 로고
    • The presumed potassium carrier Trk2p in Saccharomyces cerevisiae determines an H+-dependent, K+-independent current
    • Bihler, H., Gaber, R. F., Slayman, C. L., and Bertl, A. (1999) The presumed potassium carrier Trk2p in Saccharomyces cerevisiae determines an H+-dependent, K+-independent current. FEBS Lett. 447, 115-120
    • (1999) FEBS Lett. , vol.447 , pp. 115-120
    • Bihler, H.1    Gaber, R.F.2    Slayman, C.L.3    Bertl, A.4
  • 32
    • 84873109967 scopus 로고    scopus 로고
    • Activation of an essential calcium signaling pathway in Saccharomyces cerevisiae by Kch1 and Kch2, putative low-affinity potassium transporters
    • Stefan, C. P., Zhang, N., Sokabe, T., Rivetta, A., Slayman, C. L., Montell, C., and Cunningham, K. W. (2013) Activation of an essential calcium signaling pathway in Saccharomyces cerevisiae by Kch1 and Kch2, putative low-affinity potassium transporters. Eukaryot. Cell 12, 204-214
    • (2013) Eukaryot. Cell , vol.12 , pp. 204-214
    • Stefan, C.P.1    Zhang, N.2    Sokabe, T.3    Rivetta, A.4    Slayman, C.L.5    Montell, C.6    Cunningham, K.W.7
  • 33
    • 0035933859 scopus 로고    scopus 로고
    • Stalk segment 5 of the yeast plasma membrane H+-ATPase: Mutational evidence for a role in glucose regulation
    • Miranda, M., Allen, K. E., Pardo, J. P., and Slayman, C. W. (2001) Stalk segment 5 of the yeast plasma membrane H+-ATPase: mutational evidence for a role in glucose regulation. J. Biol. Chem. 276, 22485-22490
    • (2001) J. Biol. Chem. , vol.276 , pp. 22485-22490
    • Miranda, M.1    Allen, K.E.2    Pardo, J.P.3    Slayman, C.W.4
  • 34
    • 84876853816 scopus 로고    scopus 로고
    • Coordination of K+ transporters in neurospora: TRK1 is scarce and constitutive, while HAK1 is abundant and highly regulated
    • Rivetta, A., Allen, K. E., Slayman, C. W., and Slayman, C. L. (2013) Coordination of K+ transporters in neurospora: TRK1 is scarce and constitutive, while HAK1 is abundant and highly regulated. Eukaryot. Cell 12, 684-696
    • (2013) Eukaryot. Cell , vol.12 , pp. 684-696
    • Rivetta, A.1    Allen, K.E.2    Slayman, C.W.3    Slayman, C.L.4
  • 37
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R. D., Schiestl, R. H., Willems, A. R., and Woods, R. A. (1995) Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11, 355-360
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 38
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., and Boeke, J. D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115-132
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 40
    • 84868206086 scopus 로고    scopus 로고
    • Glycosylatable GFP as a compartment-specific membrane topology reporter
    • Lee, H., Min, J., von Heijne, G., and Kim, H. (2012) Glycosylatable GFP as a compartment-specific membrane topology reporter. Biochem. Biophys. Res. Commun. 427, 780-784
    • (2012) Biochem. Biophys. Res. Commun. , vol.427 , pp. 780-784
    • Lee, H.1    Min, J.2    Von Heijne, G.3    Kim, H.4
  • 41
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., Müller, R., and Funk, M. (1995) Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156, 119-122
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Müller, R.2    Funk, M.3
  • 42
    • 46349083026 scopus 로고    scopus 로고
    • The distributions, mechanisms, and structures of metabolite-binding riboswitches
    • Barrick, J. E., and Breaker, R. R. (2007) The distributions, mechanisms, and structures of metabolite-binding riboswitches. Genome Biol. 8, R239
    • (2007) Genome Biol. , vol.8 , pp. R239
    • Barrick, J.E.1    Breaker, R.R.2
  • 43
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • Heijne, G. (1986) The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5, 3021-3027
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Heijne, G.1
  • 44
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 45
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction-the Phobius web server
    • Käll, L., Krogh, A., and Sonnhammer, E. L. (2007) Advantages of combined transmembrane topology and signal peptide prediction-the Phobius web server. Nucleic Acids Res. 35, W429-W432
    • (2007) Nucleic Acids Res. , vol.35 , pp. W429-W432
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 46
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • Pei, J., Kim, B.-H., and Grishin, N. V. (2008) PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res. 36, 2295-2300
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.-H.2    Grishin, N.V.3
  • 48
    • 84907334066 scopus 로고    scopus 로고
    • Bacterial fluoride resistance, Fluc channels, and the weak acid accumulation effect
    • Ji, C., Stockbridge, R. B., and Miller, C. (2014) Bacterial fluoride resistance, Fluc channels, and the weak acid accumulation effect. J. Gen. Physiol. 144, 257-261
    • (2014) J. Gen. Physiol. , vol.144 , pp. 257-261
    • Ji, C.1    Stockbridge, R.B.2    Miller, C.3
  • 49
    • 0023078709 scopus 로고
    • Potassium-proton symport in Neurospora: Kinetic control by pH and membrane potential
    • Blatt, M. R., Rodriguez-Navarro, A., and Slayman, C. L. (1987) Potassium-proton symport in Neurospora: kinetic control by pH and membrane potential. J. Membr. Biol. 98, 169-189
    • (1987) J. Membr. Biol. , vol.98 , pp. 169-189
    • Blatt, M.R.1    Rodriguez-Navarro, A.2    Slayman, C.L.3
  • 50
    • 0022550268 scopus 로고
    • Electrophysiological properties of Achlya hyphae: Ionic currents studied by intracellular potential recording
    • Kropf, D. L. (1986) Electrophysiological properties of Achlya hyphae: ionic currents studied by intracellular potential recording. J. Cell Biol. 102, 1209-1216
    • (1986) J. Cell Biol. , vol.102 , pp. 1209-1216
    • Kropf, D.L.1
  • 51
    • 2642607849 scopus 로고    scopus 로고
    • Ectopic potassium uptake in trk1 trk2 mutants of Saccharomyces cerevisiae correlates with a highly hyperpolarized membrane potential
    • Madrid, R., Gómez, M. J., Ramos, J., and Rodríguez-Navarro, A. (1998) Ectopic potassium uptake in trk1 trk2 mutants of Saccharomyces cerevisiae correlates with a highly hyperpolarized membrane potential. J. Biol. Chem. 273, 14838-14844
    • (1998) J. Biol. Chem. , vol.273 , pp. 14838-14844
    • Madrid, R.1    Gómez, M.J.2    Ramos, J.3    Rodríguez-Navarro, A.4
  • 52
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang, Y., Lemieux, M. J., Song, J., Auer, M., and Wang, D.-N. (2003) Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301, 616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.-N.5
  • 53
    • 70349588813 scopus 로고    scopus 로고
    • Structural basis of substrate selectivity in the glycerol-3-phosphate: Phosphate antiporter GlpT
    • Law, C. J., Enkavi, G., Wang, D.-N., and Tajkhorshid, E. (2009) Structural basis of substrate selectivity in the glycerol-3-phosphate: phosphate antiporter GlpT. Biophys J. 97, 1346-1353
    • (2009) Biophys J. , vol.97 , pp. 1346-1353
    • Law, C.J.1    Enkavi, G.2    Wang, D.-N.3    Tajkhorshid, E.4
  • 54
    • 84899927742 scopus 로고    scopus 로고
    • Why have small multidrug resistance proteins not evolved into fused, internally duplicated structures?
    • Lloris-Garcerá, P., Seppälä, S., Slusky, J. S., Rapp, M., and von Heijne, G. (2014) Why have small multidrug resistance proteins not evolved into fused, internally duplicated structures? J. Mol. Biol. 426, 2246-2254
    • (2014) J. Mol. Biol. , vol.426 , pp. 2246-2254
    • Lloris-Garcerá, P.1    Seppälä, S.2    Slusky, J.S.3    Rapp, M.4    Von Heijne, G.5
  • 55
    • 0032817780 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: Role of glycine in transmembrane helix association
    • Javadpour, M. M., Eilers, M., Groesbeek, M., and Smith, S. O. (1999) Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophys. J. 77, 1609-1618
    • (1999) Biophys. J. , vol.77 , pp. 1609-1618
    • Javadpour, M.M.1    Eilers, M.2    Groesbeek, M.3    Smith, S.O.4
  • 56
    • 0035367173 scopus 로고    scopus 로고
    • Helical membrane proteins: Diversity of functions in the context of simple architecture
    • Ubarretxena-Belandia, I., and Engelman, D. M. (2001) Helical membrane proteins: diversity of functions in the context of simple architecture. Curr. Opin. Struct. Biol. 11, 370-376
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 370-376
    • Ubarretxena-Belandia, I.1    Engelman, D.M.2
  • 57
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • Muth, T. R., and Schuldiner, S. (2000) A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE. EMBO J. 19, 234-240
    • (2000) EMBO J. , vol.19 , pp. 234-240
    • Muth, T.R.1    Schuldiner, S.2
  • 58
    • 0034051663 scopus 로고    scopus 로고
    • An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli
    • Yerushalmi, H., and Schuldiner, S. (2000) An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli. J. Biol. Chem. 275, 5264-5269
    • (2000) J. Biol. Chem. , vol.275 , pp. 5264-5269
    • Yerushalmi, H.1    Schuldiner, S.2
  • 59
    • 84882627597 scopus 로고    scopus 로고
    • Role of the central arginine R133 toward the ion selectivity of the phosphate specific channel OprP: Effects of charge and solvation
    • Modi, N., Bárcena-Uribarri, I., Bains, M., Benz, R., Hancock, R. E., and Kleinekathöfer, U. (2013) Role of the central arginine R133 toward the ion selectivity of the phosphate specific channel OprP: effects of charge and solvation. Biochemistry 52, 5522-5532
    • (2013) Biochemistry , vol.52 , pp. 5522-5532
    • Modi, N.1    Bárcena-Uribarri, I.2    Bains, M.3    Benz, R.4    Hancock, R.E.5    Kleinekathöfer, U.6


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