메뉴 건너뛰기




Volumn 7, Issue 5, 2012, Pages

Cell wall trapping of autocrine peptides for human G-protein-coupled receptors on the yeast cell surface

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; HYBRID PROTEIN; SIGNAL PEPTIDE; PEPTIDE; PHEROMONE;

EID: 84862108519     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0037136     Document Type: Article
Times cited : (24)

References (36)
  • 1
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human β2 adrenergic G-protein-coupled receptor
    • Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, et al. (2007) Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 450: 383-387.
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1    Choi, H.J.2    Rosenbaum, D.M.3    Kobilka, T.S.4    Thian, F.S.5
  • 3
    • 77951247950 scopus 로고    scopus 로고
    • Protein-protein interactions and selection: yeast-based approaches that exploit guanine nucleotide-binding protein signaling
    • Ishii J, Fukuda N, Tanaka T, Ogino C, Kondo A, (2010) Protein-protein interactions and selection: yeast-based approaches that exploit guanine nucleotide-binding protein signaling. FEBS J 277: 1982-1995.
    • (2010) FEBS J , vol.277 , pp. 1982-1995
    • Ishii, J.1    Fukuda, N.2    Tanaka, T.3    Ogino, C.4    Kondo, A.5
  • 4
    • 61649096359 scopus 로고    scopus 로고
    • G-protein-coupled receptor-focused drug discovery using a target class platform approach
    • Heilker R, Wolff M, Tautermann CS, Bieler M, (2009) G-protein-coupled receptor-focused drug discovery using a target class platform approach. Drug Discov Today 14: 231-240.
    • (2009) Drug Discov Today , vol.14 , pp. 231-240
    • Heilker, R.1    Wolff, M.2    Tautermann, C.S.3    Bieler, M.4
  • 5
    • 77953711307 scopus 로고    scopus 로고
    • Importance of asparagine residues at positions 13 and 26 on the amino-terminal domain of human somatostatin receptor subtype-5 in signalling
    • Togawa S, Ishii J, Ishikura A, Tanaka T, Ogino C, et al. (2010) Importance of asparagine residues at positions 13 and 26 on the amino-terminal domain of human somatostatin receptor subtype-5 in signalling. J Biochem 147: 867-873.
    • (2010) J Biochem , vol.147 , pp. 867-873
    • Togawa, S.1    Ishii, J.2    Ishikura, A.3    Tanaka, T.4    Ogino, C.5
  • 6
    • 77953707787 scopus 로고    scopus 로고
    • Control of signalling properties of human somatostatin receptor subtype-5 by additional signal sequences on its amino-terminus in yeast
    • Iguchi Y, Ishii J, Nakayama H, Ishikura A, Izawa K, et al. (2010) Control of signalling properties of human somatostatin receptor subtype-5 by additional signal sequences on its amino-terminus in yeast. J Biochem 147: 875-884.
    • (2010) J Biochem , vol.147 , pp. 875-884
    • Iguchi, Y.1    Ishii, J.2    Nakayama, H.3    Ishikura, A.4    Izawa, K.5
  • 7
    • 80051546549 scopus 로고    scopus 로고
    • Amplification of agonist stimulation of human G-protein-coupled receptor signaling in yeast
    • Fukuda N, Ishii J, Kaishima M, Kondo A, (2011) Amplification of agonist stimulation of human G-protein-coupled receptor signaling in yeast. Anal Biochem 417: 182-187.
    • (2011) Anal Biochem , vol.417 , pp. 182-187
    • Fukuda, N.1    Ishii, J.2    Kaishima, M.3    Kondo, A.4
  • 8
    • 84858743541 scopus 로고    scopus 로고
    • Transplantation of the GAL regulon into G-protein signaling circuitry in yeast
    • Ryo S, Ishii J, Iguchi Y, Fukuda N, Kondo A, (2012) Transplantation of the GAL regulon into G-protein signaling circuitry in yeast. Anal Biochem 424: 27-31.
    • (2012) Anal Biochem , vol.424 , pp. 27-31
    • Ryo, S.1    Ishii, J.2    Iguchi, Y.3    Fukuda, N.4    Kondo, A.5
  • 9
    • 33947399187 scopus 로고    scopus 로고
    • Rapid identification of functionally critical amino acids in a G protein-coupled receptor
    • Li B, Scarselli M, Knudsen CD, Kim SK, Jacobson KA, et al. (2007) Rapid identification of functionally critical amino acids in a G protein-coupled receptor. Nat Methods 4: 169-174.
    • (2007) Nat Methods , vol.4 , pp. 169-174
    • Li, B.1    Scarselli, M.2    Knudsen, C.D.3    Kim, S.K.4    Jacobson, K.A.5
  • 10
    • 0033025734 scopus 로고    scopus 로고
    • C5a receptor activation. Genetic identification of critical residues in four transmembrane helices
    • Baranski TJ, Herzmark P, Lichtarge O, Gerber BO, Trueheart J, et al. (1999) C5a receptor activation. Genetic identification of critical residues in four transmembrane helices. J Biol Chem 274: 15757-15765.
    • (1999) J Biol Chem , vol.274 , pp. 15757-15765
    • Baranski, T.J.1    Herzmark, P.2    Lichtarge, O.3    Gerber, B.O.4    Trueheart, J.5
  • 11
    • 0034045526 scopus 로고    scopus 로고
    • Genetic immobilization of proteins on the yeast cell surface
    • Ueda M, Tanaka A, (2000) Genetic immobilization of proteins on the yeast cell surface. Biotechnol Adv 18: 121-140.
    • (2000) Biotechnol Adv , vol.18 , pp. 121-140
    • Ueda, M.1    Tanaka, A.2
  • 12
    • 1642340053 scopus 로고    scopus 로고
    • Yeast cell-surface display-applications of molecular display
    • Kondo A, Ueda M, (2004) Yeast cell-surface display-applications of molecular display. Appl Microbiol Biotechnol 64: 28-40.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 28-40
    • Kondo, A.1    Ueda, M.2
  • 13
    • 59449089510 scopus 로고    scopus 로고
    • Molecular display technology using yeast-arming technology
    • Shibasaki S, Maeda H, Ueda M, (2009) Molecular display technology using yeast-arming technology. Anal Sci 25: 41-49.
    • (2009) Anal Sci , vol.25 , pp. 41-49
    • Shibasaki, S.1    Maeda, H.2    Ueda, M.3
  • 14
    • 34648832245 scopus 로고    scopus 로고
    • Yeast surface display for protein engineering and characterization
    • Gai SA, Wittrup KD, (2007) Yeast surface display for protein engineering and characterization. Curr Opin Struct Biol 17: 467-473.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 467-473
    • Gai, S.A.1    Wittrup, K.D.2
  • 16
    • 0030659017 scopus 로고    scopus 로고
    • Genetic immobilization of cellulase on the cell surface of Saccharomyces cerevisiae
    • Murai T, Ueda M, Atomi H, Shibasaki Y, Kamasawa N, et al. (1997) Genetic immobilization of cellulase on the cell surface of Saccharomyces cerevisiae. Appl Microbiol Biotechnol 48: 499-503.
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 499-503
    • Murai, T.1    Ueda, M.2    Atomi, H.3    Shibasaki, Y.4    Kamasawa, N.5
  • 17
    • 0037212985 scopus 로고    scopus 로고
    • Long anchor using Flo1 protein enhances reactivity of cell surface-displayed glucoamylase to polymer substrates
    • Sato N, Matsumoto T, Ueda M, Tanaka A, Fukuda H, et al. (2002) Long anchor using Flo1 protein enhances reactivity of cell surface-displayed glucoamylase to polymer substrates. Appl Microbiol Biotechnol 60: 469-474.
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 469-474
    • Sato, N.1    Matsumoto, T.2    Ueda, M.3    Tanaka, A.4    Fukuda, H.5
  • 18
    • 0036727246 scopus 로고    scopus 로고
    • Construction of yeast strains with high cell surface lipase activity by using novel display systems based on the Flo1p flocculation functional domain
    • Matsumoto T, Fukuda H, Ueda M, Tanaka A, Kondo A, (2002) Construction of yeast strains with high cell surface lipase activity by using novel display systems based on the Flo1p flocculation functional domain. Appl Environ Microbiol 68: 4517-4522.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4517-4522
    • Matsumoto, T.1    Fukuda, H.2    Ueda, M.3    Tanaka, A.4    Kondo, A.5
  • 19
    • 2442510169 scopus 로고    scopus 로고
    • Construction of system for localization of target protein in yeast periplasm using invertase
    • Tanino T, Matsumoto T, Fukuda H, Kondo A, (2004) Construction of system for localization of target protein in yeast periplasm using invertase. J Mol Catal, B Enzym 28: 259-264.
    • (2004) J Mol Catal, B Enzym , vol.28 , pp. 259-264
    • Tanino, T.1    Matsumoto, T.2    Fukuda, H.3    Kondo, A.4
  • 20
    • 0034760935 scopus 로고    scopus 로고
    • Development of novel whole-cell immunoadsorbents by yeast surface display of the IgG-binding domain
    • Nakamura Y, Shibasaki S, Ueda M, Tanaka A, Fukuda H, et al. (2001) Development of novel whole-cell immunoadsorbents by yeast surface display of the IgG-binding domain. Appl Microbiol Biotechnol 57: 500-505.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 500-505
    • Nakamura, Y.1    Shibasaki, S.2    Ueda, M.3    Tanaka, A.4    Fukuda, H.5
  • 21
    • 56649111369 scopus 로고    scopus 로고
    • Highly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method
    • Antipov E, Cho AE, Wittrup KD, Klibanov AM, (2008) Highly L and D enantioselective variants of horseradish peroxidase discovered by an ultrahigh-throughput selection method. Proc Natl Acad Sci USA 105: 17694-17699.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17694-17699
    • Antipov, E.1    Cho, A.E.2    Wittrup, K.D.3    Klibanov, A.M.4
  • 22
    • 0037318058 scopus 로고    scopus 로고
    • Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library
    • Feldhaus MJ, Siegel RW, Opresko LK, Coleman JR, Feldhaus JM, et al. (2003) Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library. Nat Biotechnol 21: 163-170.
    • (2003) Nat Biotechnol , vol.21 , pp. 163-170
    • Feldhaus, M.J.1    Siegel, R.W.2    Opresko, L.K.3    Coleman, J.R.4    Feldhaus, J.M.5
  • 23
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • Boder ET, Midelfort KS, Wittrup KD, (2000) Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc Natl Acad Sci USA 97: 10701-10705.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 24
    • 0000923617 scopus 로고
    • Common signal transduction system shared by STE2 and STE3 in haploid cells of Saccharomyces cerevisiae: autocrine cell-cycle arrest results from forced expression of STE2
    • Nakayama N, Miyajima A, Arai K, (1987) Common signal transduction system shared by STE2 and STE3 in haploid cells of Saccharomyces cerevisiae: autocrine cell-cycle arrest results from forced expression of STE2. EMBO J 6: 249-254.
    • (1987) EMBO J , vol.6 , pp. 249-254
    • Nakayama, N.1    Miyajima, A.2    Arai, K.3
  • 25
    • 0024710930 scopus 로고
    • The yeast STE12 protein binds to the DNA sequence mediating pheromone induction'
    • Dolan JW, Kirkman C, Fields S, (1989) The yeast STE12 protein binds to the DNA sequence mediating pheromone induction. Proc Natl Acad Sc. USA 86: 5703-5707.
    • (1989) Proc Natl Acad Sc USA , vol.86 , pp. 5703-5707
    • Dolan, J.W.1    Kirkman, C.2    Fields, S.3
  • 27
    • 0015595922 scopus 로고
    • Primary structure of somatostatin, a hypothalamic peptide that inhibits the secretion of pituitary growth hormone
    • Burgus R, Ling N, Butcher M, Guillemin R, (1973) Primary structure of somatostatin, a hypothalamic peptide that inhibits the secretion of pituitary growth hormone. Proc Natl Acad Sci USA 70: 684-688.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 684-688
    • Burgus, R.1    Ling, N.2    Butcher, M.3    Guillemin, R.4
  • 28
    • 43449084942 scopus 로고    scopus 로고
    • Yeast-based fluorescence reporter assay of G protein-coupled receptor signalling for flow cytometric screening: FAR1-disruption recovers loss of episomal plasmid caused by signalling in yeast
    • Ishii J, Tanaka T, Matsumura S, Tatematsu K, Kuroda S, et al. (2008) Yeast-based fluorescence reporter assay of G protein-coupled receptor signalling for flow cytometric screening: FAR1-disruption recovers loss of episomal plasmid caused by signalling in yeast. J Biochem 143: 667-674.
    • (2008) J Biochem , vol.143 , pp. 667-674
    • Ishii, J.1    Tanaka, T.2    Matsumura, S.3    Tatematsu, K.4    Kuroda, S.5
  • 29
    • 0031058930 scopus 로고    scopus 로고
    • Pheromone signalling and polarized morphogenesis in yeast
    • Leberer E, Thomas DY, Whiteway M, (1997) Pheromone signalling and polarized morphogenesis in yeast. Curr Opin Genet Dev 7: 59-66.
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 59-66
    • Leberer, E.1    Thomas, D.Y.2    Whiteway, M.3
  • 30
    • 77953254182 scopus 로고    scopus 로고
    • Functional single-cell analyses: flow cytometry and cell sorting of microbial populations and communities
    • Müller S, Nebe-von-Caron G, (2010) Functional single-cell analyses: flow cytometry and cell sorting of microbial populations and communities. FEMS Microbiol Rev 34: 554-587.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 554-587
    • Müller, S.1    Nebe-von-Caron, G.2
  • 31
    • 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 CB, Davies A, Cost GJ, Caputo E, Li J, et al. (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
  • 32
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D, St Jean A, Woods RA, Schiestl RH, (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20: 1425.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 33
    • 0023800138 scopus 로고
    • The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin
    • MacKay VL, Welch SK, Insley MY, Manney TR, Holly J, et al. (1988) The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin. Proc Natl Acad Sci USA 85: 55-59.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 55-59
    • MacKay, V.L.1    Welch, S.K.2    Insley, M.Y.3    Manney, T.R.4    Holly, J.5
  • 34
    • 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 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
  • 35
    • 33747182213 scopus 로고    scopus 로고
    • Quantitative and dynamic analyses of G protein-coupled receptor signaling in yeast using Fus1, enhanced green fluorescence protein (EGFP), and His3 fusion protein
    • Ishii J, Matsumura S, Kimura S, Tatematsu K, Kuroda S, et al. (2006) Quantitative and dynamic analyses of G protein-coupled receptor signaling in yeast using Fus1, enhanced green fluorescence protein (EGFP), and His3 fusion protein. Biotechnol Prog 22: 954-960.
    • (2006) Biotechnol Prog , vol.22 , pp. 954-960
    • Ishii, J.1    Matsumura, S.2    Kimura, S.3    Tatematsu, K.4    Kuroda, S.5
  • 36
    • 67651165085 scopus 로고    scopus 로고
    • A simple and immediate method for simultaneously evaluating expression level and plasmid maintenance in yeast
    • Ishii J, Izawa K, Matsumura S, Wakamura K, Tanino T, et al. (2009) A simple and immediate method for simultaneously evaluating expression level and plasmid maintenance in yeast. J Biochem 145: 701-708.
    • (2009) J Biochem , vol.145 , pp. 701-708
    • Ishii, J.1    Izawa, K.2    Matsumura, S.3    Wakamura, K.4    Tanino, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.