메뉴 건너뛰기




Volumn 390, Issue 1, 2005, Pages 145-155

Subcellular localization and functional expression of the glycerol uptake protein 1 (GUP1) of Saccharomyces cerevisiae tagged with green fluorescent protein

Author keywords

Endocytosis; Green fluorescent protein (GFP); GUP1; Localization; Protein topology; Yeast

Indexed keywords

FUNGI; GLYCEROL; YEAST;

EID: 23944501318     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20042045     Document Type: Article
Times cited : (18)

References (51)
  • 2
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • Hohmann, S. (2002) Osmotic stress signaling and osmoadaptation in yeasts. Microbiol. Mol. Biol. 66, 300-372
    • (2002) Microbiol. Mol. Biol. , vol.66 , pp. 300-372
    • Hohmann, S.1
  • 3
    • 0026596917 scopus 로고
    • Physiology of osmotolerance in fungi
    • Blomberg, A. and Adler, L. (1992) Physiology of osmotolerance in fungi. Adv. Microb. Physiol. 33, 145-212
    • (1992) Adv. Microb. Physiol. , vol.33 , pp. 145-212
    • Blomberg, A.1    Adler, L.2
  • 4
    • 0002987402 scopus 로고    scopus 로고
    • Osmolytes and cell volume regulation: Physiological and evolutionary principles
    • (Hoffmann, J. F. and Jamieson J. D., eds.), Oxford University Press, New York
    • Somero, G. N. and Yancey, P. H. (1997) Osmolytes and cell volume regulation: physiological and evolutionary principles. In Handbook of Physiology, Section 14: Cell Physiology (Hoffmann, J. F. and Jamieson J. D., eds.), pp. 441-484, Oxford University Press, New York
    • (1997) Handbook of Physiology, Section 14: Cell Physiology , pp. 441-484
    • Somero, G.N.1    Yancey, P.H.2
  • 5
    • 0030725132 scopus 로고    scopus 로고
    • Contribution to the physiological characterization of glycerol active uptake in Saccharomyces cerevisiae
    • Lages, F. and Lucas, C. (1997) Contribution to the physiological characterization of glycerol active uptake in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1322, 8-18
    • (1997) Biochim. Biophys. Acta , vol.1322 , pp. 8-18
    • Lages, F.1    Lucas, C.2
  • 6
    • 0030842569 scopus 로고    scopus 로고
    • Osmoresponsive proteins and functional assessment strategies in Saccharomyces cerevisiae
    • Blomberg, A. (1997) Osmoresponsive proteins and functional assessment strategies in Saccharomyces cerevisiae. Electrophoresis 18, 1429-1440
    • (1997) Electrophoresis , vol.18 , pp. 1429-1440
    • Blomberg, A.1
  • 7
    • 0033909398 scopus 로고    scopus 로고
    • GUP1 and its close homologue GUP2, encoding multimembrane-spanning proteins involved in active glycerol uptake in Saccharomyces cerevisiae
    • Holst, B., Lunde, C., Lages, F., Oliveira, R., Lucas, C. and Kielland-Brandt, M. C. (2000) GUP1 and its close homologue GUP2, encoding multimembrane-spanning proteins involved in active glycerol uptake in Saccharomyces cerevisiae. Mol. Microbiol. 37, 108-124
    • (2000) Mol. Microbiol. , vol.37 , pp. 108-124
    • Holst, B.1    Lunde, C.2    Lages, F.3    Oliveira, R.4    Lucas, C.5    Kielland-Brandt, M.C.6
  • 8
    • 0034717265 scopus 로고    scopus 로고
    • A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol esterification in yeast
    • Oelkers, P., Tinkelenberg, A., Erdeniz, N., Cromley, D., Billheimer, J. T. and Sturley, S. L. (2000) A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol esterification in yeast. J. Biol. Chem. 275, 15609-15612
    • (2000) J. Biol. Chem. , vol.275 , pp. 15609-15612
    • Oelkers, P.1    Tinkelenberg, A.2    Erdeniz, N.3    Cromley, D.4    Billheimer, J.T.5    Sturley, S.L.6
  • 9
    • 0036320668 scopus 로고    scopus 로고
    • Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae
    • Bonangelino, C. J., Chavez, E. M. and Bonifacino, J. S. (2002) Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol. Biol. Cell 13, 2486-2501
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2486-2501
    • Bonangelino, C.J.1    Chavez, E.M.2    Bonifacino, J.S.3
  • 10
    • 0035162931 scopus 로고    scopus 로고
    • A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae
    • Ni, L. and Snyder, M. (2001) A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae. Mol. Biol. Cell 12, 2147-2170
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2147-2170
    • Ni, L.1    Snyder, M.2
  • 11
    • 0030669393 scopus 로고    scopus 로고
    • Classification of all putative permeases and other membrane plurispanners of the major facilitator superfamily encoded by the complete genome of Saccharomyces cerevisiae
    • Nelissen, B., De Wachter, R. and Goffeau, A. (1997) Classification of all putative permeases and other membrane plurispanners of the major facilitator superfamily encoded by the complete genome of Saccharomyces cerevisiae. FEMS Microbiol. Rev. 21, 113-134
    • (1997) FEMS Microbiol. Rev. , vol.21 , pp. 113-134
    • Nelissen, B.1    De Wachter, R.2    Goffeau, A.3
  • 12
    • 0034161499 scopus 로고    scopus 로고
    • A superfamily of membrane-bound O-acyltransferases with implications for Wnt signaling
    • Hofmann, K. (2000) A superfamily of membrane-bound O-acyltransferases with implications for Wnt signaling. Trends Biochem. Sci. 25, 111-112
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 111-112
    • Hofmann, K.1
  • 13
    • 0036727680 scopus 로고    scopus 로고
    • Phylogenetic classification of transporters and other membrane proteins from Saccharomyces cerevisiae
    • De Hertogh, B., Carvajal, E., Talla, E., Dujon, B., Baret, P. and Goffeau, A. (2002) Phylogenetic classification of transporters and other membrane proteins from Saccharomyces cerevisiae. Funct. Integr. Genomics 2, 154-170
    • (2002) Funct. Integr. Genomics , vol.2 , pp. 154-170
    • De Hertogh, B.1    Carvajal, E.2    Talla, E.3    Dujon, B.4    Baret, P.5    Goffeau, A.6
  • 14
    • 2342667381 scopus 로고    scopus 로고
    • New insights on glycerol transport in Saccharomyces cerevisiae
    • Neves, L., Lages, F. and Lucas, C. (2004) New insights on glycerol transport in Saccharomyces cerevisiae. FEBS Lett. 565, 160-162
    • (2004) FEBS Lett. , vol.565 , pp. 160-162
    • Neves, L.1    Lages, F.2    Lucas, C.3
  • 15
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein. Annu. Rev. Biochem. 67,509-544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 16
    • 2442553594 scopus 로고    scopus 로고
    • Imaging green fluorescent protein fusions in living fission yeast cells
    • Tran, P. T., Paoletti, A. and Chang, F. (2004) Imaging green fluorescent protein fusions in living fission yeast cells. Methods 33, 220-225
    • (2004) Methods , vol.33 , pp. 220-225
    • Tran, P.T.1    Paoletti, A.2    Chang, F.3
  • 19
    • 0031050445 scopus 로고    scopus 로고
    • Yeast-enhanced green fluorescent protein (yEGFP) a reporter of gene expression in Candida albicans
    • Cormack, B. P., Bertram, G., Egerton, M., Gow, N. A., Falkow, S. and Brown, A. J. (1997) Yeast-enhanced green fluorescent protein (yEGFP) a reporter of gene expression in Candida albicans. Microbiology 143, 303-311
    • (1997) Microbiology , vol.143 , pp. 303-311
    • Cormack, B.P.1    Bertram, G.2    Egerton, M.3    Gow, N.A.4    Falkow, S.5    Brown, A.J.6
  • 20
    • 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
  • 21
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, III, A., Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippserif P. and Pringle, J. R. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippserif, P.7    Pringle, J.R.8
  • 22
    • 0028884177 scopus 로고
    • Precise gene disruption in Saccharomyces cerevisiae by double fusion polymerase chain reaction
    • Amberg, D. C., Botstein, D. and Beasley, E. M. (1995) Precise gene disruption in Saccharomyces cerevisiae by double fusion polymerase chain reaction. Yeast 11, 1275-1280
    • (1995) Yeast , vol.11 , pp. 1275-1280
    • Amberg, D.C.1    Botstein, D.2    Beasley, E.M.3
  • 23
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae
    • Wach, A. (1996) PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12, 259-265
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 24
    • 0036566150 scopus 로고    scopus 로고
    • Utilization of green fluorescent protein as a marker for studying the expression and turnover of the monocarboxylate permease Jen1p of Saccharomyces cerevisiae
    • Paiva, S., Kruckeberg, A. L. and Casal, M. (2002) Utilization of green fluorescent protein as a marker for studying the expression and turnover of the monocarboxylate permease Jen1p of Saccharomyces cerevisiae. Biochem. J. 363, 737-744
    • (2002) Biochem. J. , vol.363 , pp. 737-744
    • Paiva, S.1    Kruckeberg, A.L.2    Casal, M.3
  • 25
  • 26
    • 0028137213 scopus 로고
    • Detection of rice tungro bacilliform virus gene products in vivo
    • Hay, J., Grieco, F., Druka, A., Pinner, M., Lee, S. C. and Hull, R. (1994) Detection of rice tungro bacilliform virus gene products in vivo. Virology 205, 430-437
    • (1994) Virology , vol.205 , pp. 430-437
    • Hay, J.1    Grieco, F.2    Druka, A.3    Pinner, M.4    Lee, S.C.5    Hull, R.6
  • 28
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., Field, C. and Schekman, R. (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell (Cambridge, Mass.) 21, 205-215
    • (1980) Cell (Cambridge, Mass.) , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 29
    • 0021712774 scopus 로고
    • Defective plasma membrane assembly in yeast secretory mutants
    • Tschopp, J., Esmon, P. C. and Schekman, R. (1984) Defective plasma membrane assembly in yeast secretory mutants. J. Bacteriol. 160, 966-970
    • (1984) J. Bacteriol. , vol.160 , pp. 966-970
    • Tschopp, J.1    Esmon, P.C.2    Schekman, R.3
  • 30
    • 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. and 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
  • 31
    • 0033560732 scopus 로고    scopus 로고
    • Functional expression, quantification and cellular localization of the Hxt2 hexose transporter of Saccharomyces cerevisiae tagged with the green fluorescent protein
    • Kruckeberg, A. L., Ye, L., Berden, J. A. and van Dam, K. (1999) Functional expression, quantification and cellular localization of the Hxt2 hexose transporter of Saccharomyces cerevisiae tagged with the green fluorescent protein. Biochem. J. 339, 299-307
    • (1999) Biochem. J. , vol.339 , pp. 299-307
    • Kruckeberg, A.L.1    Ye, L.2    Berden, J.A.3    Van Dam, K.4
  • 32
    • 0035697196 scopus 로고    scopus 로고
    • Functional analysis of the hexose transporter homologue HXT5 in Saccharomyces cerevisiae
    • Diderich, J. A., Schuurmans, J. M., Van Gaalen, M. C., Kruckeberg, A. L. and Van Dam, K. (2001) Functional analysis of the hexose transporter homologue HXT5 in Saccharomyces cerevisiae. Yeast 18, 1515-1524
    • (2001) Yeast , vol.18 , pp. 1515-1524
    • Diderich, J.A.1    Schuurmans, J.M.2    Van Gaalen, M.C.3    Kruckeberg, A.L.4    Van Dam, K.5
  • 33
    • 0034768946 scopus 로고    scopus 로고
    • Expression and activity of the Hxt7 high-affinity hexose transporter of Saccharomyces cerevisiae
    • Ye, L., Berden, J. A., van Dam, K. and Kruckeberg, A. L. (2001) Expression and activity of the Hxt7 high-affinity hexose transporter of Saccharomyces cerevisiae. Yeast 18, 1257-1267
    • (2001) Yeast , vol.18 , pp. 1257-1267
    • Ye, L.1    Berden, J.A.2    Van Dam, K.3    Kruckeberg, A.L.4
  • 34
    • 0032738114 scopus 로고    scopus 로고
    • Intracellular localization of an active green fluorescent protein-tagged Pho84 phosphate permease in Saccharomyces cerevisiae
    • Petersson, J., Pattison, J., Kruckeberg, A. L., Berden, J. A. and Persson, B. L. (1999) Intracellular localization of an active green fluorescent protein-tagged Pho84 phosphate permease in Saccharomyces cerevisiae. FEBS Lett. 462, 37-42
    • (1999) FEBS Lett. , vol.462 , pp. 37-42
    • Petersson, J.1    Pattison, J.2    Kruckeberg, A.L.3    Berden, J.A.4    Persson, B.L.5
  • 35
    • 0345255797 scopus 로고    scopus 로고
    • Visualization of protein compartmentation within the plasma membrane of living yeast cells
    • Malinska, K., Malinsky, J., Opekarova, M. and Tanner, W. (2003) Visualization of protein compartmentation within the plasma membrane of living yeast cells. Mol. Biol. Cell 14, 4427-4436
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4427-4436
    • Malinska, K.1    Malinsky, J.2    Opekarova, M.3    Tanner, W.4
  • 36
    • 0035113706 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae cyclin Clb2p is targeted to multiple subcellular locations by cis- and trans-acting determinants
    • Hood, J. K., Hwang, W. W. and Silver, P. A. (2001) The Saccharomyces cerevisiae cyclin Clb2p is targeted to multiple subcellular locations by cis- and trans-acting determinants. J. Cell Sci. 114, 589-597
    • (2001) J. Cell Sci. , vol.114 , pp. 589-597
    • Hood, J.K.1    Hwang, W.W.2    Silver, P.A.3
  • 37
    • 0034955239 scopus 로고    scopus 로고
    • Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: Crucial role of Doa4p ubiquitin isopeptidase
    • Dupre, S. and 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
  • 38
    • 0017056930 scopus 로고
    • Catabolite inactivation in yeast
    • Holzer, H. (1976) Catabolite inactivation in yeast. Trends Biochem. Sci. 1,178-181
    • (1976) Trends Biochem. Sci. , vol.1 , pp. 178-181
    • Holzer, H.1
  • 39
    • 0022534114 scopus 로고
    • Two yeast mutants defective in endocytosis are defective in pheromone response
    • Chvatchko, Y., Howald, I. and Riezman, H. (1986) Two yeast mutants defective in endocytosis are defective in pheromone response. Cell (Cambridge, Mass.) 46, 355-364
    • (1986) Cell (Cambridge, Mass.) , vol.46 , pp. 355-364
    • Chvatchko, Y.1    Howald, I.2    Riezman, H.3
  • 40
    • 0042205318 scopus 로고    scopus 로고
    • The role of ubiquitin in down-regulation and intracellular sorting of membrane proteins: Insights from yeast
    • Horak, J. (2003) The role of ubiquitin in down-regulation and intracellular sorting of membrane proteins: insights from yeast. Biochim. Biophys. Acta 1614, 139-155
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 139-155
    • Horak, J.1
  • 41
    • 0023853298 scopus 로고
    • Secretory vesicles externalize the major plasma membrane ATPase in yeast
    • Holcomb, C. L., Hansen, W. J., Etcheverry, T. and Schekman, R. (1988) Secretory vesicles externalize the major plasma membrane ATPase in yeast. J. Cell Biol. 106, 641-648
    • (1988) J. Cell Biol. , vol.106 , pp. 641-648
    • Holcomb, C.L.1    Hansen, W.J.2    Etcheverry, T.3    Schekman, R.4
  • 42
    • 0035983407 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Big1p, a putative endoplasmic reticulum membrane protein required for normal levels of cell wall beta-1,6-glucan
    • Azuma, M., Levinson, J. N., Page, N. and Bussey, H. (2002) Saccharomyces cerevisiae Big1p, a putative endoplasmic reticulum membrane protein required for normal levels of cell wall beta-1,6-glucan. Yeast 19, 783-793
    • (2002) Yeast , vol.19 , pp. 783-793
    • Azuma, M.1    Levinson, J.N.2    Page, N.3    Bussey, H.4
  • 44
    • 3843140548 scopus 로고    scopus 로고
    • A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis
    • Ki, J. J., Kawarasaki, Y., Gam, J., Harvey, B. R., Iverson, B. L. and Georgiou, G. (2004) A periplasmic fluorescent reporter protein and its application in high-throughput membrane protein topology analysis. J. Mol. Biol. 341, 901-909
    • (2004) J. Mol. Biol. , vol.341 , pp. 901-909
    • Ki, J.J.1    Kawarasaki, Y.2    Gam, J.3    Harvey, B.R.4    Iverson, B.L.5    Georgiou, G.6
  • 45
    • 0033178350 scopus 로고    scopus 로고
    • Cytological evidence that the C-terminus of carnitine palmitoyltransferase I is on the cytosolic face of the mitochondrial outer membrane
    • van der Leij, F. R., Kram, A. M., Bartelds, B., Roelofsen, H., Smid, G. B., Takens, J., Zammit, V. A. and Kuipers, J. R. (1999) Cytological evidence that the C-terminus of carnitine palmitoyltransferase I is on the cytosolic face of the mitochondrial outer membrane. Biochem. J. 341, 777-784
    • (1999) Biochem. J. , vol.341 , pp. 777-784
    • Van Der Leij, F.R.1    Kram, A.M.2    Bartelds, B.3    Roelofsen, H.4    Smid, G.B.5    Takens, J.6    Zammit, V.A.7    Kuipers, J.R.8
  • 46
    • 0033679053 scopus 로고    scopus 로고
    • In vivo N-glycosylation of the mep2 high-affinity ammonium transporter of Saccharomyces cerevisiae reveals an extracytosolic N-terminus
    • Marini, A. M. and Andre, B. (2000) In vivo N-glycosylation of the mep2 high-affinity ammonium transporter of Saccharomyces cerevisiae reveals an extracytosolic N-terminus. Mol. Microbiol. 38, 552-564
    • (2000) Mol. Microbiol. , vol.38 , pp. 552-564
    • Marini, A.M.1    Andre, B.2
  • 47
    • 0037444804 scopus 로고    scopus 로고
    • The N-terminus of the human copper transporter 1 (hCTR1) is localized extracellularly, and interacts with itself
    • Klomp, A. E., Juijn, J. A., van der Gun, L. T., van den Berg, I. E., Berger, R. and Klomp, L. W. (2003) The N-terminus of the human copper transporter 1 (hCTR1) is localized extracellularly, and interacts with itself. Biochem. J. 370, 881-889
    • (2003) Biochem. J. , vol.370 , pp. 881-889
    • Klomp, A.E.1    Juijn, J.A.2    Van Der Gun, L.T.3    Van Den Berg, I.E.4    Berger, R.5    Klomp, L.W.6
  • 48
    • 0026315381 scopus 로고
    • In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using beta-lactamase gene fusions
    • Cartwright, C. P. and Tipper, D. J. (1991) In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using beta-lactamase gene fusions. Mol. Cell. Biol. 11, 2620-2628
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2620-2628
    • Cartwright, C.P.1    Tipper, D.J.2
  • 50
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas, B. J. and Rothstein, R. (1989) Elevated recombination rates in transcriptionally active DNA. Cell (Cambridge, Mass.) 56, 619-630
    • (1989) Cell (Cambridge, Mass.) , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2
  • 51
    • 0025823999 scopus 로고
    • Expression of the yeast plasma membrane [H+]ATPase in secretory vescicles. A new strategy for directed mutagenesis
    • Nakamoto, R. K., Rao, R. and Slayman, C. W. (1991) Expression of the yeast plasma membrane [H+]ATPase in secretory vescicles. A new strategy for directed mutagenesis. J. Biol. Chem. 266, 7940-7949
    • (1991) J. Biol. Chem. , vol.266 , pp. 7940-7949
    • Nakamoto, R.K.1    Rao, R.2    Slayman, C.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.