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Volumn 9, Issue 1, 2010, Pages 173-183

Differential roles of the glycogen-binding domains of β subunits in regulation of the Snf1 kinase complex

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; GLUCOSE; GLYCOGEN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; ISOENZYME; MULTIPROTEIN COMPLEX; PROTEIN SERINE THREONINE KINASE; PROTEIN SUBUNIT; SACCHAROMYCES CEREVISIAE PROTEIN; SIP1 PROTEIN, S CEREVISIAE; SNF1 RELATED PROTEIN KINASES; SNF1-RELATED PROTEIN KINASES;

EID: 75649125966     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00267-09     Document Type: Article
Times cited : (20)

References (34)
  • 1
    • 2942568007 scopus 로고    scopus 로고
    • Key role of Ser562/661 in Snf1-dependent regulation of Cat8p in Saccharomyces cerevisiae and Kluyveromyces lactis
    • Charbon, G., et al. 2004. Key role of Ser562/661 in Snf1-dependent regulation of Cat8p in Saccharomyces cerevisiae and Kluyveromyces lactis. Mol. Cell. Biol. 24:4083-4091.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4083-4091
    • Charbon, G.1
  • 2
    • 0029944966 scopus 로고    scopus 로고
    • Regulation of 5 -AMP-activated protein kinase activity by the noncatalytic beta and gamma subunits
    • Dyck, J. R., et al. 1996. Regulation of 5 -AMP-activated protein kinase activity by the noncatalytic beta and gamma subunits. J. Biol. Chem. 271: 17798-17803.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17798-17803
    • Dyck, J.R.1
  • 3
    • 31544468889 scopus 로고    scopus 로고
    • Purification and characterization of the three Snf1activating kinases of Saccharomyces cerevisiae
    • Elbing, K., et al. 2006. Purification and characterization of the three Snf1activating kinases of Saccharomyces cerevisiae. Biochem. J. 393:797-805.
    • (2006) Biochem. J. , vol.393 , pp. 797-805
    • Elbing, K.1
  • 4
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami, S., et al. 2003. Global analysis of protein expression in yeast. Nature 425:737-741.
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 5
    • 0016414490 scopus 로고
    • β-D-Fructofuranoside fructohydrolase from yeast
    • Goldstein, A., and J. O. Lampen. 1975. β-D-Fructofuranoside fructohydrolase from yeast. Methods Enzymol. 42C:504-511.
    • (1975) Methods Enzymol. , pp. 504-511
    • Goldstein, A.1    Lampen, J.O.2
  • 6
    • 34648828532 scopus 로고    scopus 로고
    • AMP-activated/SNF1 protein kinases: Conserved guardians of cellular energy
    • Hardie, D. G. 2007. AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy. Nat. Rev. Mol. Cell Biol. 8:774-785.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 774-785
    • Hardie, D.G.1
  • 7
    • 38449110592 scopus 로고    scopus 로고
    • SNF1/AMPK pathways in yeast
    • Hedbacker, K., and M. Carlson. 2008. SNF1/AMPK pathways in yeast. Front. Biosci. 13:2408-2420.
    • (2008) Front. Biosci. , vol.13 , pp. 2408-2420
    • Hedbacker, K.1    Carlson, M.2
  • 8
    • 4444311163 scopus 로고    scopus 로고
    • Pak1 protein kinase regulates activation and nuclear localization of Snf1-Gal83 protein kinase
    • Hedbacker, K., et al. 2004. Pak1 protein kinase regulates activation and nuclear localization of Snf1-Gal83 protein kinase. Mol. Cell. Biol. 24:8255-8263.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8255-8263
    • Hedbacker, K.1
  • 9
    • 34447128162 scopus 로고    scopus 로고
    • Regulation of snf1 protein kinase in response to environmental stress
    • Hong, S. P., and M. Carlson. 2007. Regulation of snf1 protein kinase in response to environmental stress. J. Biol. Chem. 282:16838-16845.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16838-16845
    • Hong, S.P.1    Carlson, M.2
  • 10
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov, V. V. 2000. Rapid and reliable protein extraction from yeast. Yeast 16:857-860.
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 11
    • 33750979827 scopus 로고    scopus 로고
    • The evolution of putative starch-binding domains
    • Machovic, M., and S. Janecek. 2006. The evolution of putative starch-binding domains. FEBS Lett. 580:6349-6356.
    • (2006) Febs Lett. , vol.580 , pp. 6349-6356
    • Machovic, M.1    Janecek, S.2
  • 12
    • 57849090443 scopus 로고    scopus 로고
    • The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor
    • McBride, A., et al. 2009. The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor. Cell Metab. 9:23-34.
    • (2009) Cell Metab. , vol.9 , pp. 23-34
    • McBride, A.1
  • 13
    • 0035965277 scopus 로고    scopus 로고
    • Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit
    • McCartney, R. R., and M. C. Schmidt. 2001. Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit. J. Biol. Chem. 276:36460-36466.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36460-36466
    • McCartney, R.R.1    Schmidt, M.C.2
  • 14
    • 0028600673 scopus 로고
    • Substrate specificity of protein kinase CK2
    • Meggio, F., et al. 1994. Substrate specificity of protein kinase CK2. Cell. Mol. Biol. Res. 40:401-409.
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 401-409
    • Meggio, F.1
  • 15
    • 50349099673 scopus 로고    scopus 로고
    • Roles of the glycogen-binding domain and Snf4 in glucose inhibition of SNF1 protein kinase
    • Momcilovic, M., et al. 2008. Roles of the glycogen-binding domain and Snf4 in glucose inhibition of SNF1 protein kinase. J. Biol. Chem. 283:19521-19529.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19521-19529
    • Momcilovic, M.1
  • 16
    • 0037184937 scopus 로고    scopus 로고
    • Purification and characterization of Snf1 kinase complexes containing a defined beta subunit composition
    • Nath, N., et al. 2002. Purification and characterization of Snf1 kinase complexes containing a defined beta subunit composition. J. Biol. Chem. 277: 50403-50408.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50403-50408
    • Nath, N.1
  • 17
    • 0043071497 scopus 로고    scopus 로고
    • Mammalian AMP-activated protein kinase: Functional, heterotrimeric complexes by co-expression of subunits in Escherichia coli
    • Neumann, D., et al. 2003. Mammalian AMP-activated protein kinase: functional, heterotrimeric complexes by co-expression of subunits in Escherichia coli. Protein Expr. Purif. 30:230-237.
    • (2003) Protein Expr. Purif. , vol.30 , pp. 230-237
    • Neumann, D.1
  • 18
    • 33847643776 scopus 로고    scopus 로고
    • Quantification of mRNA using real-time RT-PCR
    • Nolan, T., et al. 2006. Quantification of mRNA using real-time RT-PCR. Nat. Protoc. 1:1559-1582.
    • (2006) Nat. Protoc. , vol.1 , pp. 1559-1582
    • Nolan, T.1
  • 19
    • 0037799908 scopus 로고    scopus 로고
    • AMPK beta subunit targets metabolic stress sensing to glycogen
    • Polekhina, G., et al. 2003. AMPK beta subunit targets metabolic stress sensing to glycogen. Curr. Biol. 13:867-871.
    • (2003) Curr. Biol. , vol.13 , pp. 867-871
    • Polekhina, G.1
  • 20
    • 26444608572 scopus 로고    scopus 로고
    • Structural basis for glycogen recognition by AMP-activated protein kinase
    • Polekhina, G., et al. 2005. Structural basis for glycogen recognition by AMP-activated protein kinase. Structure 13:1453-1462.
    • (2005) Structure , vol.13 , pp. 1453-1462
    • Polekhina, G.1
  • 21
    • 0029610003 scopus 로고
    • CAT5, a new gene necessary for derepression of gluconeogenic enzymes in Saccharomyces cerevisiae
    • Proft, M., et al. 1995. CAT5, a new gene necessary for derepression of gluconeogenic enzymes in Saccharomyces cerevisiae. EMBO J. 14:6116-6126.
    • (1995) Embo J. , vol.14 , pp. 6116-6126
    • Proft, M.1
  • 22
    • 38049174646 scopus 로고    scopus 로고
    • Access denied: Snf1 activation loop phosphorylation is controlled by availability of the phosphorylated threonine 210 to the PP1 phosphatase
    • Rubenstein, E. M., et al. 2008. Access denied: Snf1 activation loop phosphorylation is controlled by availability of the phosphorylated threonine 210 to the PP1 phosphatase. J. Biol. Chem. 283:222-230.
    • (2008) J. Biol. Chem. , vol.283 , pp. 222-230
    • Rubenstein, E.M.1
  • 23
    • 34147152841 scopus 로고    scopus 로고
    • Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    • Sanders, M. J., et al. 2007. Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade. Biochem. J. 403:139-148.
    • (2007) Biochem. J. , vol.403 , pp. 139-148
    • Sanders, M.J.1
  • 24
    • 0034665041 scopus 로고    scopus 로고
    • Beta-subunits of Snf1 kinase are required for kinase function and substrate definition
    • Schmidt, M. C., and R. R. McCartney. 2000. Beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J. 19:4936-4943.
    • (2000) Embo J. , vol.19 , pp. 4936-4943
    • Schmidt, M.C.1    McCartney, R.R.2
  • 25
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen, T. D., and K. J. Livak. 2008. Analyzing real-time PCR data by the comparative C(T) method. Nat. Protoc. 3:1101-1108.
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 26
    • 85047691317 scopus 로고    scopus 로고
    • CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations
    • Scott, J. W., et al. 2004. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. J. Clin. Invest. 113:274-284.
    • (2004) J. Clin. Invest. , vol.113 , pp. 274-284
    • Scott, J.W.1
  • 27
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 28
    • 0032768263 scopus 로고    scopus 로고
    • The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1
    • Smith, F. C., et al. 1999. The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1. FEBS Lett. 453:219-223.
    • (1999) Febs Lett. , vol.453 , pp. 219-223
    • Smith, F.C.1
  • 29
    • 0025772724 scopus 로고
    • Identification of an epitope on the P and V proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics
    • Southern, J. A., et al. 1991. Identification of an epitope on the P and V proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics. J. Gen. Virol. 72:1551-1557.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1551-1557
    • Southern, J.A.1
  • 30
    • 0036905343 scopus 로고    scopus 로고
    • Active Snf1 protein kinase inhibits expression of the Saccharomyces cerevisiae HXT1 glucose transporter gene
    • Tomas-Cobos, L., and P. Sanz. 2002. Active Snf1 protein kinase inhibits expression of the Saccharomyces cerevisiae HXT1 glucose transporter gene. Biochem. J. 368:657-663.
    • (2002) Biochem. J. , vol.368 , pp. 657-663
    • Tomas-Cobos, L.1    Sanz, P.2
  • 31
    • 0031740335 scopus 로고    scopus 로고
    • Snf1 protein kinase regulates phosphorylation of the Mig1 repressor in Saccharomyces cerevisiae
    • Treitel, M. A., et al. 1998. Snf1 protein kinase regulates phosphorylation of the Mig1 repressor in Saccharomyces cerevisiae. Mol. Cell. Biol. 18:6273-6280.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6273-6280
    • Treitel, M.A.1
  • 32
    • 0035338114 scopus 로고    scopus 로고
    • Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism
    • Vincent, O., et al. 2001. Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev. 15:1104-1114.
    • (2001) Genes Dev. , vol.15 , pp. 1104-1114
    • Vincent, O.1
  • 33
    • 34848840368 scopus 로고    scopus 로고
    • Structural basis for AMP binding to mammalian AMP-activated protein kinase
    • Xiao, B., et al. 2007. Structural basis for AMP binding to mammalian AMP-activated protein kinase. Nature 449:496-500.
    • (2007) Nature , vol.449 , pp. 496-500
    • Xiao, B.1
  • 34
    • 65349177200 scopus 로고    scopus 로고
    • AMPK: An emerging drug target for diabetes and the metabolic syndrome
    • Zhang, B. B., et al. 2009. AMPK: an emerging drug target for diabetes and the metabolic syndrome. Cell Metab. 9:407-416.
    • (2009) Cell Metab. , vol.9 , pp. 407-416
    • Zhang, B.B.1


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