메뉴 건너뛰기




Volumn 4, Issue 6, 2005, Pages 1041-1049

Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p

Author keywords

[No Author keywords available]

Indexed keywords

ATG16 PROTEIN, S CEREVISIAE; CARRIER PROTEIN; CATION TRANSPORT PROTEIN; FUNGAL PROTEIN; HYGROMYCIN B; MEMBRANE PROTEIN; NHA1 PROTEIN, S CEREVISIAE; PHOSPHOPROTEIN; PHOSPHOPROTEIN PHOSPHATASE; POTASSIUM; RUBIDIUM; SACCHAROMYCES CEREVISIAE PROTEIN; SAP155 PROTEIN, S CEREVISIAE; SIT4 PROTEIN, S CEREVISIAE; SMALL NUCLEAR RIBONUCLEOPROTEIN; SODIUM PROTON EXCHANGE PROTEIN; TRANSCRIPTION FACTOR;

EID: 20444490360     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.4.6.1041-1049.2005     Document Type: Article
Times cited : (14)

References (51)
  • 2
    • 0036148514 scopus 로고    scopus 로고
    • Role of the Nha1 antiporter in regulating K+ influx in Saccharomyces cerevisiae
    • Banuelos, M. A., M. C. Ruiz, A. Jimenez, J.-L. Souciet, S. Potier, and J. Ramos. 2002. Role of the Nha1 antiporter in regulating K+ influx in Saccharomyces cerevisiae. Yeast 19:9-15.
    • (2002) Yeast , vol.19 , pp. 9-15
    • Banuelos, M.A.1    Ruiz, M.C.2    Jimenez, A.3    Souciet, J.-L.4    Potier, S.5    Ramos, J.6
  • 4
    • 0037238864 scopus 로고    scopus 로고
    • Characterization of potassium transport in wild-type and isogenic yeast strains carrying all combinations of trk1, trk2, and tok1 null mutations
    • Bertl, A., J. Ramos, J. Ludwig, H. Lichtenberg-Frate, J. Reid, H. Bihler, F. Calero, P. Martinez, and P. O. Ljungdahl. 2003. Characterization of potassium transport in wild-type and isogenic yeast strains carrying all combinations of trk1, trk2, and tok1 null mutations. Mol. Microbiol. 47:767-780.
    • (2003) Mol. Microbiol. , vol.47 , pp. 767-780
    • Bertl, A.1    Ramos, J.2    Ludwig, J.3    Lichtenberg-Frate, H.4    Reid, J.5    Bihler, H.6    Calero, F.7    Martinez, P.8    Ljungdahl, P.O.9
  • 5
    • 0036467320 scopus 로고    scopus 로고
    • Low-affinity potassium uptake by Saccharomyces cerevisiae is mediated by NSC1, a calcium-blocked non-specific cation channel
    • Bihler, H., C. L. Slayman, and A. Bertl. 2002. Low-affinity potassium uptake by Saccharomyces cerevisiae is mediated by NSC1, a calcium-blocked non-specific cation channel. Biochim. Biophys. Acta 1558:109-118.
    • (2002) Biochim. Biophys. Acta , vol.1558 , pp. 109-118
    • Bihler, H.1    Slayman, C.L.2    Bertl, A.3
  • 6
    • 0032584621 scopus 로고    scopus 로고
    • NSC1: A novel high-current inward rectifier for cations in the plasma membrane of Saccharomyces cerevisiae
    • Bihler, H., C. L. Slayman, and A. Bertl. 1998. NSC1: a novel high-current inward rectifier for cations in the plasma membrane of Saccharomyces cerevisiae. FEES Lett. 432:59-64.
    • (1998) FEES Lett. , vol.432 , pp. 59-64
    • Bihler, H.1    Slayman, C.L.2    Bertl, A.3
  • 7
    • 0032872353 scopus 로고    scopus 로고
    • The yeast PRS3 gene is required for cell integrity, cell cycle arrest upon nutrient deprivation, ion homeostasis and the proper organization of the actin cytoskeleton
    • Binley, K. M., P. A. Radcliffe, J. Trevethick, K. A. Duffy, and P. E. Sudbery. 1999. The yeast PRS3 gene is required for cell integrity, cell cycle arrest upon nutrient deprivation, ion homeostasis and the proper organization of the actin cytoskeleton. Yeast 15:1459-1469.
    • (1999) Yeast , vol.15 , pp. 1459-1469
    • Binley, K.M.1    Radcliffe, P.A.2    Trevethick, J.3    Duffy, K.A.4    Sudbery, P.E.5
  • 8
    • 0020640158 scopus 로고
    • Construction of high copy yeast vectors using 2-micron circle sequences
    • Broach, J. R. 1983. Construction of high copy yeast vectors using 2-micron circle sequences. Methods Enzymol. 101:307-325.
    • (1983) Methods Enzymol. , vol.101 , pp. 307-325
    • Broach, J.R.1
  • 9
    • 0033019059 scopus 로고    scopus 로고
    • The yeast Ser/Thr phosphatases Sit4 and Ppz1 play opposite roles in regulation of the cell cycle
    • Clotet, J., E. Gar, M. Aldea, and J. Arino. 1999. The yeast Ser/Thr phosphatases Sit4 and Ppz1 play opposite roles in regulation of the cell cycle. Mol. Cell. Biol. 19:2408-2415.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2408-2415
    • Clotet, J.1    Gar, E.2    Aldea, M.3    Arino, J.4
  • 10
    • 0029166109 scopus 로고
    • Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3
    • Ferrando, A., S. J. Kron, G. Rios, G. R. Fink, and R. Serrano. 1995. Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3. Mol. Cell. Biol. 15:5470-5481.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5470-5481
    • Ferrando, A.1    Kron, S.J.2    Rios, G.3    Fink, G.R.4    Serrano, R.5
  • 11
    • 0026463553 scopus 로고
    • Molecular genetics of yeast ion transport
    • Gaber, R. F. 1992. Molecular genetics of yeast ion transport. Int. Rev. Cytol. 137A:299-353.
    • (1992) Int. Rev. Cytol. , vol.137 A , pp. 299-353
    • Gaber, R.F.1
  • 12
    • 0024042922 scopus 로고
    • TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cerevisiae
    • Gaber, R. F., C. A. Styles, and G. R. Fink. 1988. TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cerevisiae. Mol. Cell. Biol. 8:2848-2859.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2848-2859
    • Gaber, R.F.1    Styles, C.A.2    Fink, G.R.3
  • 13
    • 0024595608 scopus 로고
    • Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation
    • Heuser, J. E., and R. G. Anderson. 1989. Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation. J. Cell Biol. 108:389-400.
    • (1989) J. Cell Biol. , vol.108 , pp. 389-400
    • Heuser, J.E.1    Anderson, R.G.2
  • 14
    • 0022781503 scopus 로고
    • Yeast/Escherichia coli shuttle vectors with multiple unique restriction sites
    • Hill, J. E., A. M. Myers, T. J. Koerner, and A. Tzagoloff. 1986. Yeast/Escherichia coli shuttle vectors with multiple unique restriction sites. Yeast 2:163-167.
    • (1986) Yeast , vol.2 , pp. 163-167
    • Hill, J.E.1    Myers, A.M.2    Koerner, T.J.3    Tzagoloff, A.4
  • 15
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 16
    • 0035697437 scopus 로고    scopus 로고
    • Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin
    • Jablonowski, D., A. R. Butler, L. Fichtner, D. Gardiner, R. Schaffrath, and M. J. R. Stark. 2001. Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin. Genetics 159:1479-1489.
    • (2001) Genetics , vol.159 , pp. 1479-1489
    • Jablonowski, D.1    Butler, A.R.2    Fichtner, L.3    Gardiner, D.4    Schaffrath, R.5    Stark, M.J.R.6
  • 18
    • 0025822954 scopus 로고
    • + transporters in Saccharomyces cerevisiae
    • + transporters in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:4266-4273.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4266-4273
    • Ko, C.H.1    Gaber, R.F.2
  • 19
    • 0020626609 scopus 로고
    • Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts
    • Larkin, J. M., M. S. Brown, J. L. Goldstein, and R. G. Anderson. 1983. Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts. Cell 33:273-285.
    • (1983) Cell , vol.33 , pp. 273-285
    • Larkin, J.M.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.4
  • 20
    • 0022401444 scopus 로고
    • Modulation of intracellular potassium and ATP: Effects on coated pit function in fibroblasts and hepatocytes
    • Larkin, J. M., W. C. Donzell, and R. G. Anderson. 1985. Modulation of intracellular potassium and ATP: effects on coated pit function in fibroblasts and hepatocytes. J. Cell Physiol. 124:372-378.
    • (1985) J. Cell Physiol. , vol.124 , pp. 372-378
    • Larkin, J.M.1    Donzell, W.C.2    Anderson, R.G.3
  • 21
    • 0022899025 scopus 로고
    • Potassium-dependent assembly of coated pits: New coated pits form as planar clathrin lattices
    • Larkin, J. M., W. C. Donzell, and R. G. Anderson. 1986. Potassium-dependent assembly of coated pits: new coated pits form as planar clathrin lattices. J. Cell Biol. 103:2619-2627.
    • (1986) J. Cell Biol. , vol.103 , pp. 2619-2627
    • Larkin, J.M.1    Donzell, W.C.2    Anderson, R.G.3
  • 22
    • 0017365519 scopus 로고
    • Control of protein synthesis in human fibroblasts by intracellular potassium
    • Ledbetter, M. L. S., and M. Lubin. 1977. Control of protein synthesis in human fibroblasts by intracellular potassium. Exp. Cell Res. 105:223-236.
    • (1977) Exp. Cell Res. , vol.105 , pp. 223-236
    • Ledbetter, M.L.S.1    Lubin, M.2
  • 25
    • 0347495593 scopus 로고
    • Intracellular potassium and control of protein synthesis
    • Lubin, M. 1964. Intracellular potassium and control of protein synthesis. Fed. Proc. 23:994-1001.
    • (1964) Fed. Proc. , vol.23 , pp. 994-1001
    • Lubin, M.1
  • 26
    • 0014192217 scopus 로고
    • Intracellular potassium and macromolecular synthesis in mammalian cells
    • Lubin, M. 1967. Intracellular potassium and macromolecular synthesis in mammalian cells. Nature 213:451-453.
    • (1967) Nature , vol.213 , pp. 451-453
    • Lubin, M.1
  • 27
    • 0000214972 scopus 로고
    • On the role of intracellular potassium in protein synthesis
    • Lubin, M., and H. L. Ennis. 1964. On the role of intracellular potassium in protein synthesis. Biochim. Biophys. Acta 80:614-631.
    • (1964) Biochim. Biophys. Acta , vol.80 , pp. 614-631
    • Lubin, M.1    Ennis, H.L.2
  • 28
    • 0029664530 scopus 로고    scopus 로고
    • The SAPs, a new family of proteins, associate and function positively with the SIT4 phosphatase
    • Luke, M. M., F. Della Seta, C. J. Di Como, H. Sugimoto, R. Kobayashi, and K. T. Arndt. 1996. The SAPs, a new family of proteins, associate and function positively with the SIT4 phosphatase. Mol. Cell. Biol. 16:2744-2755.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2744-2755
    • Luke, M.M.1    Della Seta, F.2    Di Como, C.J.3    Sugimoto, H.4    Kobayashi, R.5    Arndt, K.T.6
  • 29
    • 2642607849 scopus 로고    scopus 로고
    • Ectopic potassium uptake in trk1 trk2 mutants of Saccharomyces cerevisiae correlates with a highly hyperpolarized membrane potential
    • Madrid, R., M. J. Gomez, J. Ramos, and A. Rodriguez-Navarro. 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    Gomez, M.J.2    Ramos, J.3    Rodriguez-Navarro, A.4
  • 30
    • 13144249178 scopus 로고    scopus 로고
    • Physiological characterization of Saccharomyces cerevisiae kha1 deletion mutants
    • Maresova, L., and H. Sychrova. 2005. Physiological characterization of Saccharomyces cerevisiae kha1 deletion mutants. Mol. Microbiol. 55:588-600.
    • (2005) Mol. Microbiol. , vol.55 , pp. 588-600
    • Maresova, L.1    Sychrova, H.2
  • 31
    • 0034613255 scopus 로고    scopus 로고
    • Regulation of monovalent ion homeostasis and pH by the Ser-Thr protein phosphatase SIT4 in Saccharomyces cerevisiae
    • Masuda, C. A., J. Ramirez, A. Pena, and M. Montero-Lomeli. 2000. Regulation of monovalent ion homeostasis and pH by the Ser-Thr protein phosphatase SIT4 in Saccharomyces cerevisiae. J. Biol. Chem. 275:30957-30961.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30957-30961
    • Masuda, C.A.1    Ramirez, J.2    Pena, A.3    Montero-Lomeli, M.4
  • 32
    • 0032931992 scopus 로고    scopus 로고
    • A novel mechanism of ion homeostasis and salt tolerance in yeast: The Hal4 and Hal5 protein kinases modulate the Trk1-Trk2 potassium transporter
    • Mulet, J. M., M. P. Leube, S. J. Kron, G. Rios, G. R. Fink, and R. Serrano. 1999. A novel mechanism of ion homeostasis and salt tolerance in yeast: the Hal4 and Hal5 protein kinases modulate the Trk1-Trk2 potassium transporter. Mol. Cell. Biol. 19:3328-3337.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3328-3337
    • Mulet, J.M.1    Leube, M.P.2    Kron, S.J.3    Rios, G.4    Fink, G.R.5    Serrano, R.6
  • 35
    • 0028897490 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity
    • O'Brien, M. C., and D. B. McKay. 1995. How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity. J. Biol. Chem. 270:2247-2250.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2247-2250
    • O'Brien, M.C.1    McKay, D.B.2
  • 36
    • 0027473930 scopus 로고
    • Accumulation and intracellular compartmentation of lithium ions in Saccharomyces cerevisiae
    • Perkins, J., and G. M. Gadd. 1993. Accumulation and intracellular compartmentation of lithium ions in Saccharomyces cerevisiae. FEMS Microbiol. Lett. 107:255-260.
    • (1993) FEMS Microbiol. Lett. , vol.107 , pp. 255-260
    • Perkins, J.1    Gadd, G.M.2
  • 38
    • 0028008822 scopus 로고
    • TRK2 is not a low-affinity potassium transport in Saccharomyces cerevisiae
    • Ramos, J., R. Aligo, R. Haro, and A. Rodriguez-Navarro. 1994. TRK2 is not a low-affinity potassium transport in Saccharomyces cerevisiae. J. Bacteriol. 176:249-252.
    • (1994) J. Bacteriol. , vol.176 , pp. 249-252
    • Ramos, J.1    Aligo, R.2    Haro, R.3    Rodriguez-Navarro, A.4
  • 40
    • 4544333055 scopus 로고    scopus 로고
    • TOR controls transcriptional and translational programs via Sap-Sit4 protein phosphatase signaling effectors
    • Rohde, J. R., S. Campbell, S. A. Zurita-Martinez, N. S. Cutler, M. Ashe, and M. E. Cardenas. 2004. TOR controls transcriptional and translational programs via Sap-Sit4 protein phosphatase signaling effectors. Mol. Cell. Biol. 24:8332-8341.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8332-8341
    • Rohde, J.R.1    Campbell, S.2    Zurita-Martinez, S.A.3    Cutler, N.S.4    Ashe, M.5    Cardenas, M.E.6
  • 44
    • 0038201930 scopus 로고    scopus 로고
    • + antiporter carboxy-terminal tail reveals residues required for function in cell cycle
    • + antiporter carboxy-terminal tail reveals residues required for function in cell cycle. FEES Lett. 545:239-245.
    • (2003) FEES Lett. , vol.545 , pp. 239-245
    • Simon, E.1    Barcelo, A.2    Arino, J.3
  • 45
    • 0035839453 scopus 로고    scopus 로고
    • A screening for high copy suppressors of the sit4 hal3 synthetically lethal phenotype reveals a role for the yeast Nha1 antiporter in cell cycle regulation
    • Simon, E., J. Clotet, F. Calero, J. Ramos, and J. Arino. 2001. A screening for high copy suppressors of the sit4 hal3 synthetically lethal phenotype reveals a role for the yeast Nha1 antiporter in cell cycle regulation. J. Biol. Chem. 276:29740-29747.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29740-29747
    • Simon, E.1    Clotet, J.2    Calero, F.3    Ramos, J.4    Arino, J.5
  • 47
    • 0344938357 scopus 로고    scopus 로고
    • Involvement of Nha1 antiporter in regulation of intracellular pH in Saccharomyces cerevisiae
    • Sychrova, H., J. Ramirez, and A. Pena. 1999. Involvement of Nha1 antiporter in regulation of intracellular pH in Saccharomyces cerevisiae. FEMS Microbiol. Lett. 171:167-172.
    • (1999) FEMS Microbiol. Lett. , vol.171 , pp. 167-172
    • Sychrova, H.1    Ramirez, J.2    Pena, A.3
  • 48
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
    • Wilbanks, S. M., and D. B. McKay. 1995. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270:2251-2257.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 50
    • 0036500159 scopus 로고    scopus 로고
    • + and pH homeostasis: Implications for salt tolerance, cell wall integrity and cell cycle progression
    • + and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression. EMBO J. 21:920-929.
    • (2002) EMBO J. , vol.21 , pp. 920-929
    • Yenush, L.1    Mulet, J.M.2    Arino, J.3    Serrano, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.