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Volumn 6, Issue 6, 2011, Pages

Regulation of alr1 mg transporter activity by intracellular magnesium

Author keywords

[No Author keywords available]

Indexed keywords

ALR1 MAGNESIUM TRANSPORTER; AMINO TERMINAL TELOPEPTIDE; CARBOXY TERMINAL TELOPEPTIDE; CARRIER PROTEINS AND BINDING PROTEINS; COBALT; MAGNESIUM; MANGANESE; NICKEL; UNCLASSIFIED DRUG; ZINC ION; ALR1 PROTEIN, S CEREVISIAE; CATION TRANSPORT PROTEIN; MESSENGER RNA; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 79959581604     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020896     Document Type: Article
Times cited : (16)

References (89)
  • 1
    • 0027996567 scopus 로고
    • Magnesium: the fifth but forgotten electrolyte
    • Elin RJ, (1994) Magnesium: the fifth but forgotten electrolyte. Am J Clin Pathol 102: 616-622.
    • (1994) Am J Clin Pathol , vol.102 , pp. 616-622
    • Elin, R.J.1
  • 2
    • 0002138965 scopus 로고
    • Introduction to the biological chemistry of the magnesium ion
    • In: Cowan JA, editors, New York, VCH Publishers
    • Cowan JA, (1995) Introduction to the biological chemistry of the magnesium ion. In: Cowan JA, editors. The Biological Chemistry of Magnesium New York VCH Publishers pp. 1-23.
    • (1995) The Biological Chemistry of Magnesium , pp. 1-23
    • Cowan, J.A.1
  • 3
    • 0002229695 scopus 로고
    • Magnesium: an introduction to its biochemistry
    • In: Birch NJ, editors, San Diego, Academic Press Inc
    • Williams RJP, (1993) Magnesium: an introduction to its biochemistry. In: Birch NJ, editors. Magnesium and the Cell San Diego Academic Press Inc pp. 15-30.
    • (1993) Magnesium and the Cell , pp. 15-30
    • Williams, R.J.P.1
  • 5
    • 38349078268 scopus 로고    scopus 로고
    • Cell (patho)physiology of magnesium
    • Wolf FI, Trapani V, (2008) Cell (patho)physiology of magnesium. Clin Sci (Lond) 114: 27-35.
    • (2008) Clin Sci (Lond) , vol.114 , pp. 27-35
    • Wolf, F.I.1    Trapani, V.2
  • 6
    • 0035105303 scopus 로고    scopus 로고
    • The pleiotropic two-component regulatory system PhoP-PhoQ
    • Groisman EA, (2001) The pleiotropic two-component regulatory system PhoP-PhoQ. J Bacteriol 183: 1835-1842.
    • (2001) J Bacteriol , vol.183 , pp. 1835-1842
    • Groisman, E.A.1
  • 8
    • 0024589247 scopus 로고
    • Hypomagnesemia in patients in postoperative intensive care
    • Chernow B, Bamberger S, Stoiko M, Vadnais M, Mills S, et al. (1989) Hypomagnesemia in patients in postoperative intensive care. Chest 95: 391-397.
    • (1989) Chest , vol.95 , pp. 391-397
    • Chernow, B.1    Bamberger, S.2    Stoiko, M.3    Vadnais, M.4    Mills, S.5
  • 11
    • 0037421538 scopus 로고    scopus 로고
    • Role of magnesium in the pathogenesis of hypertension
    • Touyz RM, (2003) Role of magnesium in the pathogenesis of hypertension. Mol Aspects Med 24: 107-136.
    • (2003) Mol Aspects Med , vol.24 , pp. 107-136
    • Touyz, R.M.1
  • 12
    • 0346726107 scopus 로고    scopus 로고
    • Low serum magnesium predicts neurological events in patients with advanced atherosclerosis
    • Amighi J, Sabeti S, Schlager O, Mlekusch W, Exner M, et al. (2004) Low serum magnesium predicts neurological events in patients with advanced atherosclerosis. Stroke 35: 22-27.
    • (2004) Stroke , vol.35 , pp. 22-27
    • Amighi, J.1    Sabeti, S.2    Schlager, O.3    Mlekusch, W.4    Exner, M.5
  • 13
    • 0021264382 scopus 로고
    • Magnesium transport across cell membranes
    • Flatman PW, (1984) Magnesium transport across cell membranes. J Membr Biol 80: 1-14.
    • (1984) J Membr Biol , vol.80 , pp. 1-14
    • Flatman, P.W.1
  • 14
    • 0036315896 scopus 로고    scopus 로고
    • Intracellular magnesium and magnesium buffering
    • Grubbs RD, (2002) Intracellular magnesium and magnesium buffering. Biometals 15: 251-259.
    • (2002) Biometals , vol.15 , pp. 251-259
    • Grubbs, R.D.1
  • 16
    • 34548066282 scopus 로고    scopus 로고
    • Bacterial homologs of eukaryotic membrane proteins: the 2-TM-GxN family of Mg2+ transporters
    • Papp-Wallace KM, Maguire ME, (2007) Bacterial homologs of eukaryotic membrane proteins: the 2-TM-GxN family of Mg2+ transporters. Mol Membr Biol 24: 351-356.
    • (2007) Mol Membr Biol , vol.24 , pp. 351-356
    • Papp-Wallace, K.M.1    Maguire, M.E.2
  • 17
    • 36849093398 scopus 로고    scopus 로고
    • Mrs2p forms a high conductance Mg2+ selective channel in mitochondria
    • Schindl R, Weghuber J, Romanin C, Schweyen RJ, (2007) Mrs2p forms a high conductance Mg2+ selective channel in mitochondria. Biophys J 93: 3872-3883.
    • (2007) Biophys J , vol.93 , pp. 3872-3883
    • Schindl, R.1    Weghuber, J.2    Romanin, C.3    Schweyen, R.J.4
  • 18
    • 66149145111 scopus 로고    scopus 로고
    • Conditional knock-down of hMRS2 results in loss of mitochondrial Mg2+ uptake and cell death
    • Piskacek M, Zotova L, Zsurka G, Schweyen RJ, (2008) Conditional knock-down of hMRS2 results in loss of mitochondrial Mg2+ uptake and cell death. J Cell Mol Med.
    • (2008) J Cell Mol Med
    • Piskacek, M.1    Zotova, L.2    Zsurka, G.3    Schweyen, R.J.4
  • 19
    • 0035280637 scopus 로고    scopus 로고
    • The human mitochondrial Mrs2 protein functionally substitutes for its yeast homologue, a candidate magnesium transporter
    • Zsurka G, Gregan J, Schweyen RJ, (2001) The human mitochondrial Mrs2 protein functionally substitutes for its yeast homologue, a candidate magnesium transporter. Genomics 72: 158-168.
    • (2001) Genomics , vol.72 , pp. 158-168
    • Zsurka, G.1    Gregan, J.2    Schweyen, R.J.3
  • 20
    • 68149152218 scopus 로고    scopus 로고
    • Magnesium transporter AtMGT9 is essential for pollen development in Arabidopsis
    • Chen J, Li LG, Liu ZH, Yuan YJ, Guo LL, et al. (2009) Magnesium transporter AtMGT9 is essential for pollen development in Arabidopsis. Cell Res 19: 887-898.
    • (2009) Cell Res , vol.19 , pp. 887-898
    • Chen, J.1    Li, L.G.2    Liu, Z.H.3    Yuan, Y.J.4    Guo, L.L.5
  • 21
    • 57049084657 scopus 로고    scopus 로고
    • AtMGT7: An Arabidopsis Gene Encoding a Low-Affinity Magnesium Transporter
    • Mao DD, Tian LF, Li LG, Chen J, Deng PY, et al. (2008) AtMGT7: An Arabidopsis Gene Encoding a Low-Affinity Magnesium Transporter. J Integr Plant Biol 50: 1530-1538.
    • (2008) J Integr Plant Biol , vol.50 , pp. 1530-1538
    • Mao, D.D.1    Tian, L.F.2    Li, L.G.3    Chen, J.4    Deng, P.Y.5
  • 22
    • 27144470708 scopus 로고    scopus 로고
    • A putative magnesium transporter AtMRS2-11 is localized to the plant chloroplast envelope membrane system
    • Drummond R, Tutone A, Li Y, Gardner R, (2006) A putative magnesium transporter AtMRS2-11 is localized to the plant chloroplast envelope membrane system. Plant Science 170: 78-89.
    • (2006) Plant Science , vol.170 , pp. 78-89
    • Drummond, R.1    Tutone, A.2    Li, Y.3    Gardner, R.4
  • 24
    • 0035844127 scopus 로고    scopus 로고
    • The yeast plasma membrane protein Alr1 controls Mg2+ homeostasis and is subject to Mg2+-dependent control of its synthesis and degradation
    • Graschopf A, Stadler JA, Hoellerer MK, Eder S, Sieghardt M, et al. (2001) The yeast plasma membrane protein Alr1 controls Mg2+ homeostasis and is subject to Mg2+-dependent control of its synthesis and degradation. J Biol Chem 276: 16216-16222.
    • (2001) J Biol Chem , vol.276 , pp. 16216-16222
    • Graschopf, A.1    Stadler, J.A.2    Hoellerer, M.K.3    Eder, S.4    Sieghardt, M.5
  • 25
    • 33748325677 scopus 로고    scopus 로고
    • Oligomerization of the Mg2+-transport proteins Alr1p and Alr2p in yeast plasma membrane
    • Wachek M, Aichinger MC, Stadler JA, Schweyen RJ, Graschopf A, (2006) Oligomerization of the Mg2+-transport proteins Alr1p and Alr2p in yeast plasma membrane. FEBS J 273: 4236-4249.
    • (2006) FEBS J , vol.273 , pp. 4236-4249
    • Wachek, M.1    Aichinger, M.C.2    Stadler, J.A.3    Schweyen, R.J.4    Graschopf, A.5
  • 26
    • 0031893932 scopus 로고    scopus 로고
    • Overexpression of the Saccharomyces cerevisiae magnesium transport system confers resistance to aluminum ion
    • MacDiarmid CW, Gardner RC, (1998) Overexpression of the Saccharomyces cerevisiae magnesium transport system confers resistance to aluminum ion. J Biol Chem 273: 1727-1732.
    • (1998) J Biol Chem , vol.273 , pp. 1727-1732
    • MacDiarmid, C.W.1    Gardner, R.C.2
  • 27
    • 77954856723 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay maintains translational fidelity by limiting magnesium uptake
    • Johansson MJ, Jacobson A, (2010) Nonsense-mediated mRNA decay maintains translational fidelity by limiting magnesium uptake. Genes Dev 24: 1491-1495.
    • (2010) Genes Dev , vol.24 , pp. 1491-1495
    • Johansson, M.J.1    Jacobson, A.2
  • 28
    • 26944487922 scopus 로고    scopus 로고
    • Transport of magnesium and other divalent cations: evolution of the 2-TM-GxN proteins in the MIT superfamily
    • Knoop V, Groth-Malonek M, Gebert M, Eifler K, Weyand K, (2005) Transport of magnesium and other divalent cations: evolution of the 2-TM-GxN proteins in the MIT superfamily. Mol Genet Genomics 274: 205-216.
    • (2005) Mol Genet Genomics , vol.274 , pp. 205-216
    • Knoop, V.1    Groth-Malonek, M.2    Gebert, M.3    Eifler, K.4    Weyand, K.5
  • 29
    • 72449127530 scopus 로고    scopus 로고
    • MNR2 regulates intracellular magnesium storage in Saccharomyces cerevisiae
    • Pisat NP, Pandey A, Macdiarmid CW, (2009) MNR2 regulates intracellular magnesium storage in Saccharomyces cerevisiae. Genetics 183: 873-884.
    • (2009) Genetics , vol.183 , pp. 873-884
    • Pisat, N.P.1    Pandey, A.2    Macdiarmid, C.W.3
  • 30
    • 0031845660 scopus 로고    scopus 로고
    • The molecular biology of metal ion transport in Saccharomyces cerevisiae
    • Eide DJ, (1998) The molecular biology of metal ion transport in Saccharomyces cerevisiae. Annu Rev Nutr 18: 441-469.
    • (1998) Annu Rev Nutr , vol.18 , pp. 441-469
    • Eide, D.J.1
  • 31
    • 73649099463 scopus 로고    scopus 로고
    • Promoter and riboswitch control of the Mg2+ transporter MgtA from Salmonella enterica
    • Cromie MJ, Groisman EA, (2010) Promoter and riboswitch control of the Mg2+ transporter MgtA from Salmonella enterica. J Bacteriol 192: 604-607.
    • (2010) J Bacteriol , vol.192 , pp. 604-607
    • Cromie, M.J.1    Groisman, E.A.2
  • 33
    • 52649169231 scopus 로고    scopus 로고
    • Regulation of CorA Mg2+ channel function affects the virulence of Salmonella enterica serovar typhimurium
    • Papp-Wallace KM, Maguire ME, (2008) Regulation of CorA Mg2+ channel function affects the virulence of Salmonella enterica serovar typhimurium. J Bacteriol 190: 6509-6516.
    • (2008) J Bacteriol , vol.190 , pp. 6509-6516
    • Papp-Wallace, K.M.1    Maguire, M.E.2
  • 34
    • 20444485752 scopus 로고    scopus 로고
    • Post-transcriptional regulation of the yeast high affinity iron transport system
    • Felice MR, De Domenico I, Li L, Ward DM, Bartok B, et al. (2005) Post-transcriptional regulation of the yeast high affinity iron transport system. J Biol Chem 280: 22181-22190.
    • (2005) J Biol Chem , vol.280 , pp. 22181-22190
    • Felice, M.R.1    De Domenico, I.2    Li, L.3    Ward, D.M.4    Bartok, B.5
  • 35
    • 0034161957 scopus 로고    scopus 로고
    • Zinc-regulated ubiquitin conjugation signals endocytosis of the yeast ZRT1 zinc transporter
    • Gitan RS, Eide DJ, (2000) Zinc-regulated ubiquitin conjugation signals endocytosis of the yeast ZRT1 zinc transporter. Biochem J 346 Pt 2: 329-336.
    • (2000) Biochem J , vol.346 Pt , pp. 329-336
    • Gitan, R.S.1    Eide, D.J.2
  • 36
    • 33644543442 scopus 로고    scopus 로고
    • Transferrin receptor-like proteins control the degradation of a yeast metal transporter
    • Stimpson HE, Lewis MJ, Pelham HR, (2006) Transferrin receptor-like proteins control the degradation of a yeast metal transporter. EMBO J 25: 662-672.
    • (2006) EMBO J , vol.25 , pp. 662-672
    • Stimpson, H.E.1    Lewis, M.J.2    Pelham, H.R.3
  • 37
    • 0032582814 scopus 로고    scopus 로고
    • Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation
    • Gitan RS, Luo H, Rodgers J, Broderius M, Eide D, (1998) Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation. J Biol Chem 273: 28617-28624.
    • (1998) J Biol Chem , vol.273 , pp. 28617-28624
    • Gitan, R.S.1    Luo, H.2    Rodgers, J.3    Broderius, M.4    Eide, D.5
  • 38
    • 2342450002 scopus 로고    scopus 로고
    • Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast
    • Pizzirusso M, Chang A, (2004) Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast. Mol Biol Cell 15: 2401-2409.
    • (2004) Mol Biol Cell , vol.15 , pp. 2401-2409
    • Pizzirusso, M.1    Chang, A.2
  • 39
    • 0033999819 scopus 로고    scopus 로고
    • An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast
    • Luo W, Chang A, (2000) An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast. Mol Biol Cell 11: 579-592.
    • (2000) Mol Biol Cell , vol.11 , pp. 579-592
    • Luo, W.1    Chang, A.2
  • 40
    • 0030808571 scopus 로고    scopus 로고
    • Elimination of defective alpha-factor pheromone receptors
    • Jenness DD, Li Y, Tipper C, Spatrick P, (1997) Elimination of defective alpha-factor pheromone receptors. Mol Cell Biol 17: 6236-6245.
    • (1997) Mol Cell Biol , vol.17 , pp. 6236-6245
    • Jenness, D.D.1    Li, Y.2    Tipper, C.3    Spatrick, P.4
  • 41
    • 31044440408 scopus 로고    scopus 로고
    • Residues of the yeast ALR1 protein that are critical for magnesium uptake
    • Lee JM, Gardner RC, (2006) Residues of the yeast ALR1 protein that are critical for magnesium uptake. Curr Genet 49: 7-20.
    • (2006) Curr Genet , vol.49 , pp. 7-20
    • Lee, J.M.1    Gardner, R.C.2
  • 42
    • 0031592395 scopus 로고    scopus 로고
    • Regulation of cellular Mg2+ by Saccharomyces cerevisiae
    • Beeler T, Bruce K, Dunn T, (1997) Regulation of cellular Mg2+ by Saccharomyces cerevisiae. Biochim Biophys Acta 1323: 310-318.
    • (1997) Biochim Biophys Acta , vol.1323 , pp. 310-318
    • Beeler, T.1    Bruce, K.2    Dunn, T.3
  • 43
    • 0028111321 scopus 로고
    • Polyamine-sensitive magnesium transport in Saccharomyces cerevisiae
    • Maruyama T, Masuda N, Kakinuma Y, Igarashi K, (1994) Polyamine-sensitive magnesium transport in Saccharomyces cerevisiae. Biochim Biophys Acta 1194: 289-295.
    • (1994) Biochim Biophys Acta , vol.1194 , pp. 289-295
    • Maruyama, T.1    Masuda, N.2    Kakinuma, Y.3    Igarashi, K.4
  • 44
    • 0029658448 scopus 로고    scopus 로고
    • Al toxicity in yeast. A role for Mg?
    • MacDiarmid CW, Gardner RC, (1996) Al toxicity in yeast. A role for Mg? Plant Physiol 112: 1101-1109.
    • (1996) Plant Physiol , vol.112 , pp. 1101-1109
    • MacDiarmid, C.W.1    Gardner, R.C.2
  • 45
    • 67650173033 scopus 로고    scopus 로고
    • Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis
    • Hu J, Sharma M, Qin H, Gao FP, Cross TA, (2009) Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis. J Biol Chem 284: 15619-15628.
    • (2009) J Biol Chem , vol.284 , pp. 15619-15628
    • Hu, J.1    Sharma, M.2    Qin, H.3    Gao, F.P.4    Cross, T.A.5
  • 46
    • 0034595831 scopus 로고    scopus 로고
    • Cation hexaammines are selective and potent inhibitors of the CorA magnesium transport system
    • Kucharski LM, Lubbe WJ, Maguire ME, (2000) Cation hexaammines are selective and potent inhibitors of the CorA magnesium transport system. J Biol Chem 275: 16767-16773.
    • (2000) J Biol Chem , vol.275 , pp. 16767-16773
    • Kucharski, L.M.1    Lubbe, W.J.2    Maguire, M.E.3
  • 47
    • 31644451505 scopus 로고    scopus 로고
    • Nickel resistance in fission yeast associated with the magnesium transport system
    • Sarikaya AT, Akman G, Temizkan G, (2006) Nickel resistance in fission yeast associated with the magnesium transport system. Mol Biotechnol 32: 139-146.
    • (2006) Mol Biotechnol , vol.32 , pp. 139-146
    • Sarikaya, A.T.1    Akman, G.2    Temizkan, G.3
  • 49
    • 0027455339 scopus 로고
    • end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths S, Rohrer J, Crausaz F, Riezman H, (1993) end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J Cell Biol 120: 55-65.
    • (1993) J Cell Biol , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 50
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida TA, Emr SD, (1995) A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J Cell Biol 128: 779-792.
    • (1995) J Cell Biol , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 51
    • 0020696481 scopus 로고
    • Mutations in PEP4 locus of Saccharomyces cerevisiae block final step in maturation of two vacuolar hydrolases
    • Zubenko GS, Park FJ, Jones EW, (1983) Mutations in PEP4 locus of Saccharomyces cerevisiae block final step in maturation of two vacuolar hydrolases. Proc Natl Acad Sci U S A 80: 510-514.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 510-514
    • Zubenko, G.S.1    Park, F.J.2    Jones, E.W.3
  • 52
    • 0028971506 scopus 로고
    • NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein C, Springael JY, Volland C, Haguenauer-Tsapis R, Andre B, (1995) NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol Microbiol 18: 77-87.
    • (1995) Mol Microbiol , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    Andre, B.5
  • 53
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1
    • Soetens O, De Craene JO, Andre B, (2001) Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J Biol Chem 276: 43949-43957.
    • (2001) J Biol Chem , vol.276 , pp. 43949-43957
    • Soetens, O.1    de Craene, J.O.2    Andre, B.3
  • 54
    • 0036786951 scopus 로고    scopus 로고
    • Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae
    • Kaminska J, Gajewska B, Hopper AK, Zoladek T, (2002) Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae. Mol Cell Biol 22: 6946-6948.
    • (2002) Mol Cell Biol , vol.22 , pp. 6946-6948
    • Kaminska, J.1    Gajewska, B.2    Hopper, A.K.3    Zoladek, T.4
  • 55
    • 34247504273 scopus 로고    scopus 로고
    • Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway
    • Nikko E, Andre B, (2007) Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway. Traffic 8: 566-581.
    • (2007) Traffic , vol.8 , pp. 566-581
    • Nikko, E.1    Andre, B.2
  • 56
    • 0028024386 scopus 로고
    • The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast
    • Benedetti H, Raths S, Crausaz F, Riezman H, (1994) The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast. Mol Biol Cell 5: 1023-1037.
    • (1994) Mol Biol Cell , vol.5 , pp. 1023-1037
    • Benedetti, H.1    Raths, S.2    Crausaz, F.3    Riezman, H.4
  • 57
    • 0031867271 scopus 로고    scopus 로고
    • Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae
    • Springael JY, Andre B, (1998) Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae. Mol Biol Cell 9: 1253-1263.
    • (1998) Mol Biol Cell , vol.9 , pp. 1253-1263
    • Springael, J.Y.1    Andre, B.2
  • 58
    • 12644263389 scopus 로고    scopus 로고
    • A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15
    • Wendland B, McCaffery JM, Xiao Q, Emr SD, (1996) A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15. J Cell Biol 135: 1485-1500.
    • (1996) J Cell Biol , vol.135 , pp. 1485-1500
    • Wendland, B.1    McCaffery, J.M.2    Xiao, Q.3    Emr, S.D.4
  • 60
    • 0028800173 scopus 로고
    • VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper RC, Cooper AA, Yang H, Stevens TH, (1995) VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J Cell Biol 131: 603-617.
    • (1995) J Cell Biol , vol.131 , pp. 603-617
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.H.4
  • 61
    • 0030700220 scopus 로고    scopus 로고
    • Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
    • Hicke L, (1997) Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J 11: 1215-1226.
    • (1997) FASEB J , vol.11 , pp. 1215-1226
    • Hicke, L.1
  • 62
    • 45549107128 scopus 로고    scopus 로고
    • Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system
    • Payandeh J, Li C, Ramjeesingh M, Poduch E, Bear CE, et al. (2008) Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system. J Biol Chem 283: 11721-11733.
    • (2008) J Biol Chem , vol.283 , pp. 11721-11733
    • Payandeh, J.1    Li, C.2    Ramjeesingh, M.3    Poduch, E.4    Bear, C.E.5
  • 63
    • 33748031116 scopus 로고    scopus 로고
    • A structural basis for Mg2+ homeostasis and the CorA translocation cycle
    • Payandeh J, Pai EF, (2006) A structural basis for Mg2+ homeostasis and the CorA translocation cycle. EMBO J 25: 3762-3773.
    • (2006) EMBO J , vol.25 , pp. 3762-3773
    • Payandeh, J.1    Pai, E.F.2
  • 64
    • 0034721927 scopus 로고    scopus 로고
    • The family of SMF metal ion transporters in yeast cells
    • Cohen A, Nelson H, Nelson N, (2000) The family of SMF metal ion transporters in yeast cells. J Biol Chem 275: 33388-33394.
    • (2000) J Biol Chem , vol.275 , pp. 33388-33394
    • Cohen, A.1    Nelson, H.2    Nelson, N.3
  • 65
    • 0029978512 scopus 로고    scopus 로고
    • A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria
    • Supek F, Supekova L, Nelson H, Nelson N, (1996) A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria. Proc Natl Acad Sci U S A 93: 5105-5110.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5105-5110
    • Supek, F.1    Supekova, L.2    Nelson, H.3    Nelson, N.4
  • 66
    • 0033521145 scopus 로고    scopus 로고
    • Yeast SMF1 mediates H+-coupled iron uptake with concomitant uncoupled cation currents
    • Chen XZ, Peng JB, Cohen A, Nelson H, Nelson N, et al. (1999) Yeast SMF1 mediates H+-coupled iron uptake with concomitant uncoupled cation currents. J Biol Chem 274: 35089-35094.
    • (1999) J Biol Chem , vol.274 , pp. 35089-35094
    • Chen, X.Z.1    Peng, J.B.2    Cohen, A.3    Nelson, H.4    Nelson, N.5
  • 67
    • 0001352978 scopus 로고    scopus 로고
    • Post-translation control of Nramp metal transport in yeast. Role of metal ions and the BSD2 gene
    • Liu XF, Culotta VC, (1999) Post-translation control of Nramp metal transport in yeast. Role of metal ions and the BSD2 gene. J Biol Chem 274: 4863-4868.
    • (1999) J Biol Chem , vol.274 , pp. 4863-4868
    • Liu, X.F.1    Culotta, V.C.2
  • 68
    • 2942568108 scopus 로고    scopus 로고
    • Yeast Mn2+ transporter, Smf1p, is regulated by ubiquitin-dependent vacuolar protein sorting
    • Eguez L, Chung YS, Kuchibhatla A, Paidhungat M, Garrett S, (2004) Yeast Mn2+ transporter, Smf1p, is regulated by ubiquitin-dependent vacuolar protein sorting. Genetics 167: 107-117.
    • (2004) Genetics , vol.167 , pp. 107-117
    • Eguez, L.1    Chung, Y.S.2    Kuchibhatla, A.3    Paidhungat, M.4    Garrett, S.5
  • 69
    • 0037094434 scopus 로고    scopus 로고
    • Nitrogen regulation in Saccharomyces cerevisiae
    • Magasanik B, Kaiser CA, (2002) Nitrogen regulation in Saccharomyces cerevisiae. Gene 290: 1-18.
    • (2002) Gene , vol.290 , pp. 1-18
    • Magasanik, B.1    Kaiser, C.A.2
  • 70
    • 0037165612 scopus 로고    scopus 로고
    • Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease trafficking
    • Springael JY, Nikko E, Andre B, Marini AM, (2002) Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease trafficking. FEBS Lett 517: 103-109.
    • (2002) FEBS Lett , vol.517 , pp. 103-109
    • Springael, J.Y.1    Nikko, E.2    Andre, B.3    Marini, A.M.4
  • 71
    • 0035858866 scopus 로고    scopus 로고
    • Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease
    • Helliwell SB, Losko S, Kaiser CA, (2001) Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease. J Cell Biol 153: 649-662.
    • (2001) J Cell Biol , vol.153 , pp. 649-662
    • Helliwell, S.B.1    Losko, S.2    Kaiser, C.A.3
  • 72
    • 0028795584 scopus 로고
    • Targeting of the yeast plasma membrane H+-ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole
    • Chang A, Fink GR, (1995) Targeting of the yeast plasma membrane H+-ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole. J Cell Biol 128: 39-49.
    • (1995) J Cell Biol , vol.128 , pp. 39-49
    • Chang, A.1    Fink, G.R.2
  • 73
    • 33744503047 scopus 로고    scopus 로고
    • The structure of CorA: a Mg2+-selective channel
    • Maguire ME, (2006) The structure of CorA: a Mg2+-selective channel. Curr Opin Struct Biol 16: 432-438.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 432-438
    • Maguire, M.E.1
  • 75
    • 35348839586 scopus 로고    scopus 로고
    • PhosphoPep-a phosphoproteome resource for systems biology research in Drosophila Kc167 cells
    • Bodenmiller B, Malmstrom J, Gerrits B, Campbell D, Lam H, et al. (2007) PhosphoPep-a phosphoproteome resource for systems biology research in Drosophila Kc167 cells. Mol Syst Biol 3: 139.
    • (2007) Mol Syst Biol , vol.3 , pp. 139
    • Bodenmiller, B.1    Malmstrom, J.2    Gerrits, B.3    Campbell, D.4    Lam, H.5
  • 76
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz RD, St. Jean A, Woods RA, Schiestl RH, (1992) Improved method for high efficiency transformation of intact yeast cells. Nucl Acids Res 8: 1425.
    • (1992) Nucl Acids Res , vol.8 , pp. 1425
    • Gietz, R.D.1    Jean St., A.2    Woods, R.A.3    Schiestl, R.H.4
  • 77
    • 0020645052 scopus 로고
    • Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast
    • Guarente L, (1983) Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Meth Enzymol 101: 181-191.
    • (1983) Meth Enzymol , vol.101 , pp. 181-191
    • Guarente, L.1
  • 78
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad D, Hunter R, Parker R, (1992) A rapid method for localized mutagenesis of yeast genes. Yeast 8: 79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 79
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud N, Ozier-Kalogeropoulos O, Li GY, Labouesse M, Minvielle-Sebastia L, et al. (1991) A family of low and high copy replicative, integrative and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7: 609-615.
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1    Ozier-Kalogeropoulos, O.2    Li, G.Y.3    Labouesse, M.4    Minvielle-Sebastia, L.5
  • 80
    • 0023034916 scopus 로고
    • Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions
    • Myers AM, Tzagoloff A, Kinney DM, Lusty CJ, (1986) Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions. Gene 45: 299-310.
    • (1986) Gene , vol.45 , pp. 299-310
    • Myers, A.M.1    Tzagoloff, A.2    Kinney, D.M.3    Lusty, C.J.4
  • 81
    • 3042722112 scopus 로고    scopus 로고
    • Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae
    • Sheff MA, Thorn KS, (2004) Optimized cassettes for fluorescent protein tagging in Saccharomyces cerevisiae. Yeast 21: 661-670.
    • (2004) Yeast , vol.21 , pp. 661-670
    • Sheff, M.A.1    Thorn, K.S.2
  • 84
    • 3242738624 scopus 로고    scopus 로고
    • The plant CDF family member TgMTP1 from the Ni/Zn hyperaccumulator Thlaspi goesingense acts to enhance efflux of Zn at the plasma membrane when expressed in Saccharomyces cerevisiae
    • Kim D, Gustin JL, Lahner B, Persans MW, Baek D, et al. (2004) The plant CDF family member TgMTP1 from the Ni/Zn hyperaccumulator Thlaspi goesingense acts to enhance efflux of Zn at the plasma membrane when expressed in Saccharomyces cerevisiae. Plant J 39: 237-251.
    • (2004) Plant J , vol.39 , pp. 237-251
    • Kim, D.1    Gustin, J.L.2    Lahner, B.3    Persans, M.W.4    Baek, D.5
  • 85
    • 0029911793 scopus 로고    scopus 로고
    • The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation
    • Zhao H, Eide D, (1996) The yeast ZRT1 gene encodes the zinc transporter protein of a high-affinity uptake system induced by zinc limitation. Proc Natl Acad Sci USA 93: 2454-2458.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2454-2458
    • Zhao, H.1    Eide, D.2
  • 86
    • 0034955239 scopus 로고    scopus 로고
    • Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase
    • Dupre S, Haguenauer-Tsapis R, (2001) Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase. Mol Cell Biol 21: 4482-4494.
    • (2001) Mol Cell Biol , vol.21 , pp. 4482-4494
    • Dupre, S.1    Haguenauer-Tsapis, R.2
  • 87
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • Winzeler EA, Shoemaker DD, Astromoff A, Liang H, Anderson K, et al. (1999) Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285: 901-906.
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.A.1    Shoemaker, D.D.2    Astromoff, A.3    Liang, H.4    Anderson, K.5
  • 88
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan JM, Moreau V, Andre B, Volland C, Haguenauer-Tsapis R, (1996) Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J Biol Chem 271: 10946-10952.
    • (1996) J Biol Chem , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    Andre, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 89
    • 0024445121 scopus 로고
    • Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae
    • Rothman JH, Howald I, Stevens TH, (1989) Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae. EMBO J 8: 2057-2065.
    • (1989) EMBO J , vol.8 , pp. 2057-2065
    • Rothman, J.H.1    Howald, I.2    Stevens, T.H.3


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