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Volumn 9, Issue 10, 2007, Pages 1184-1191

A proteomic screen reveals SCFGrr1 targets that regulate the glycolytic-gluconeogenic switch

Author keywords

[No Author keywords available]

Indexed keywords

F BOX PROTEIN; FRUCTOSE 2,6 BISPHOSPHATASE; GLUCOSE; PROTEIN GRR1; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR PFK27; TRANSCRIPTION FACTOR SNF; TRANSCRIPTION FACTOR SNF1; TRANSCRIPTION FACTOR TYE7; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 34848817448     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1639     Document Type: Article
Times cited : (76)

References (27)
  • 1
    • 9644273891 scopus 로고    scopus 로고
    • A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
    • Willems, A. R., Schwab, M. & Tyers, M. A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim. Biophys. Acta 1695, 133-170 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 133-170
    • Willems, A.R.1    Schwab, M.2    Tyers, M.3
  • 2
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski, M. D. & Deshaies, R. J. Function and regulation of cullin-RING ubiquitin ligases. Nature Rev. Mol. Cell Biol. 6, 9-20 (2005).
    • (2005) Nature Rev. Mol. Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 3
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: Insights into a molecular machine
    • Cardozo, T. & Pagano, M. The SCF ubiquitin ligase: Insights into a molecular machine. Nature Rev. Mol. Cell Biol 5, 739-751 (2004).
    • (2004) Nature Rev. Mol. Cell Biol , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 4
    • 0025942492 scopus 로고
    • GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats
    • Flick, J. S. & Johnston, M. GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats. Mol. Cell. Biol. 11, 5101-5112 (1991).
    • (1991) Mol. Cell. Biol , vol.11 , pp. 5101-5112
    • Flick, J.S.1    Johnston, M.2
  • 5
    • 0042970750 scopus 로고    scopus 로고
    • Grr1-dependent inactivation of Mth1 mediates glucose-induced dissociation of Rgt1 from HXT gene promoters
    • Flick, K. M. et al. Grr1-dependent inactivation of Mth1 mediates glucose-induced dissociation of Rgt1 from HXT gene promoters. Mol. Biol. Cell 14, 3230-3241 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3230-3241
    • Flick, K.M.1
  • 7
    • 4344618064 scopus 로고    scopus 로고
    • The N-terminal regulatory domain of Stp1p is modular and, fused to an artificial transcription factor, confers full Ssy1p-Ptr3p-Ssy5p sensor control
    • Andreasson, C. & Ljungdahl, P. O. The N-terminal regulatory domain of Stp1p is modular and, fused to an artificial transcription factor, confers full Ssy1p-Ptr3p-Ssy5p sensor control. Mol. Cell. Biol. 24, 7503-7513 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 7503-7513
    • Andreasson, C.1    Ljungdahl, P.O.2
  • 8
    • 0028986667 scopus 로고    scopus 로고
    • Barral, Y., Jentsch, S. & Mann, C. G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast. Genes Dev. 9, 399-409 (1995).
    • Barral, Y., Jentsch, S. & Mann, C. G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast. Genes Dev. 9, 399-409 (1995).
  • 9
    • 0032530333 scopus 로고    scopus 로고
    • The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation by the SCFGrr1 complex
    • Jaquenoud, M., Gulli, M. P., Peter, K. & Peter, M. The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation by the SCFGrr1 complex. EMBO J. 17, 5360-5373 (1998).
    • (1998) EMBO J , vol.17 , pp. 5360-5373
    • Jaquenoud, M.1    Gulli, M.P.2    Peter, K.3    Peter, M.4
  • 10
    • 17844378772 scopus 로고    scopus 로고
    • Degradation of Hof1 by SCF(Grr1) is important for actomyosin contraction during cytokinesis in yeast
    • Blondel, M. et al. Degradation of Hof1 by SCF(Grr1) is important for actomyosin contraction during cytokinesis in yeast. EMBO J. 24, 1440-1452 (2005).
    • (2005) EMBO J , vol.24 , pp. 1440-1452
    • Blondel, M.1
  • 12
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • Huh, W. K. et al. Global analysis of protein localization in budding yeast. Nature 425, 686-691 (2003).
    • (2003) Nature , vol.425 , pp. 686-691
    • Huh, W.K.1
  • 13
    • 15444364763 scopus 로고    scopus 로고
    • Grr1p is required for transcriptional induction of amino acid permease genes and proper transcriptional regulation of genes in carbon metabolism of Saccharomyces cerevisiae
    • Eckert-Boulet, N., Regenberg, B. & Nielsen, J. Grr1p is required for transcriptional induction of amino acid permease genes and proper transcriptional regulation of genes in carbon metabolism of Saccharomyces cerevisiae. Curr. Genet. 47, 139-149 (2005).
    • (2005) Curr. Genet , vol.47 , pp. 139-149
    • Eckert-Boulet, N.1    Regenberg, B.2    Nielsen, J.3
  • 14
    • 17644396667 scopus 로고    scopus 로고
    • Degradation-mediated protein quality control in the nucleus
    • Gardner, R. G., Nelson, Z. W. & Gottschling, D. E. Degradation-mediated protein quality control in the nucleus. Cell 120, 803-815 (2005).
    • (2005) Cell , vol.120 , pp. 803-815
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 15
    • 0032441425 scopus 로고    scopus 로고
    • An essential function of Grr1 for the degradation of Cln2 is to act as a binding core that links Cln2 to Skp1
    • Kishi, T. & Yamao, F. An essential function of Grr1 for the degradation of Cln2 is to act as a binding core that links Cln2 to Skp1. J. Cell Sci. 111, 3655-3661 (1998).
    • (1998) J. Cell Sci , vol.111 , pp. 3655-3661
    • Kishi, T.1    Yamao, F.2
  • 16
    • 0035106567 scopus 로고    scopus 로고
    • F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its feucine-rich repeat
    • Hsiung, Y. G. et al. F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its feucine-rich repeat. Mol. Cell. Biol. 21, 2506-2520 (2001).
    • (2001) Mol. Cell. Biol , vol.21 , pp. 2506-2520
    • Hsiung, Y.G.1
  • 17
    • 0037115602 scopus 로고    scopus 로고
    • Receptor-mediated endoproteolytic activation of two transcription factors in yeast
    • Andreasson, C. & Ljungdahl, P. O. Receptor-mediated endoproteolytic activation of two transcription factors in yeast. Genes Dev. 16 3158-3172 (2002).
    • (2002) Genes Dev , vol.16 , pp. 3158-3172
    • Andreasson, C.1    Ljungdahl, P.O.2
  • 18
    • 0032735328 scopus 로고    scopus 로고
    • Fructose-2,6-bisphosphate and control of carbohydrate metabolism in eukaryotes
    • Okar, D. A. & Lange, A. J. Fructose-2,6-bisphosphate and control of carbohydrate metabolism in eukaryotes. Biofactors 10, 1-14 (1999).
    • (1999) Biofactors , vol.10 , pp. 1-14
    • Okar, D.A.1    Lange, A.J.2
  • 19
    • 0028948313 scopus 로고
    • The GCR1 requirement for yeast glycolytic gene expression is suppressed by dominant mutations in the SGC1 gene, which encodes a novel basic-helix-loop-helix protein
    • Nishi, K. et al. The GCR1 requirement for yeast glycolytic gene expression is suppressed by dominant mutations in the SGC1 gene, which encodes a novel basic-helix-loop-helix protein. Mol. Cell. Biol. 15, 2646-2653 (1995).
    • (1995) Mol. Cell. Biol , vol.15 , pp. 2646-2653
    • Nishi, K.1
  • 20
    • 1242274644 scopus 로고    scopus 로고
    • Glucose sensing and signaling in Saccharomyces cerevisiae through the Rgt2 glucose sensor and casein kinase I
    • Moriya, H. & Johnston, M. Glucose sensing and signaling in Saccharomyces cerevisiae through the Rgt2 glucose sensor and casein kinase I. Proc. Natl Acad. Sci. USA 101, 1572-1577 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1572-1577
    • Moriya, H.1    Johnston, M.2
  • 21
    • 28444460297 scopus 로고    scopus 로고
    • Global analysis of protein phosphorylation in yeast
    • Ptacek, J. et al. Global analysis of protein phosphorylation in yeast. Nature 438, 679-684 (2005).
    • (2005) Nature , vol.438 , pp. 679-684
    • Ptacek, J.1
  • 22
    • 0028942747 scopus 로고
    • Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I
    • Dale, S., Wilson, W. A., Edelman, A. M. & Hardie, D. G. Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Lett. 361, 191-195 (1995).
    • (1995) FEBS Lett , vol.361 , pp. 191-195
    • Dale, S.1    Wilson, W.A.2    Edelman, A.M.3    Hardie, D.G.4
  • 23
    • 0030824205 scopus 로고    scopus 로고
    • Signalling pathways leading to transcriptional regulation of genes involved in the activation of glycolysis in yeast
    • Goncalves, P. M., Griffioen, G., Bebelman, J. P. & Planta, R. J. Signalling pathways leading to transcriptional regulation of genes involved in the activation of glycolysis in yeast. Mol. Microbiol. 25, 483-493 (1997).
    • (1997) Mol. Microbiol , vol.25 , pp. 483-493
    • Goncalves, P.M.1    Griffioen, G.2    Bebelman, J.P.3    Planta, R.J.4
  • 24
    • 28844501882 scopus 로고    scopus 로고
    • Genome-wide surveys for phosphorylation-dependent substrates of SCF ubiquitin ligases
    • Tang, X. et al. Genome-wide surveys for phosphorylation-dependent substrates of SCF ubiquitin ligases. Methods Enzymol. 399, 433-458 (2005).
    • (2005) Methods Enzymol , vol.399 , pp. 433-458
    • Tang, X.1
  • 25
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami, S. et al. Global analysis of protein expression in yeast. Nature 425, 737-741 (2003).
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 26
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces carevisiae
    • Schmitt, M. E., Brown, T. A. & Trumpower, B. L. A rapid and simple method for preparation of RNA from Saccharomyces carevisiae. Nucleic Acids Res. 18, 3091-3092 (1990).
    • (1990) Nucleic Acids Res , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3
  • 27
    • 0031740811 scopus 로고    scopus 로고
    • Cak1 is required for Kin28 phosphorylation and activation in vivo
    • Espinoza, F. H. et al. Cak1 is required for Kin28 phosphorylation and activation in vivo. Mol. Cell. Biol. 18, 6365-6373 (1998).
    • (1998) Mol. Cell. Biol , vol.18 , pp. 6365-6373
    • Espinoza, F.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.