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Volumn 7, Issue , 2016, Pages

Structural basis of allosteric and synergistic activation of AMPK by furan-2-phosphonic derivative C2 binding

Author keywords

[No Author keywords available]

Indexed keywords

5 (5 HYDROXYL ISOXAZOL 3 YL)FURAN 2 PHOSPHONIC ACID; 6,7 DIHYDRO 4 HYDROXY 3 (2' HYDROXY 1,1' BIPHENYL 4 YL) 6 OXOTHIENO[2,3 B]PYRIDINE 5 CARBONITRILE; AMP ACTIVATED PROTEIN KINASE ALPHA1; FURAN DERIVATIVE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; NUCLEOTIDE; PHOSPHONIC ACID DERIVATIVE; UNCLASSIFIED DRUG; 5-(5-HYDROXYLISOXAZOL-3-YL)FURAN-2-PHOSPHONIC ACID; ENZYME ACTIVATOR; ISOXAZOLE DERIVATIVE;

EID: 84960416125     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10912     Document Type: Article
Times cited : (62)

References (33)
  • 1
    • 79954517977 scopus 로고    scopus 로고
    • Structure of mammalian AMPK and its regulation by ADP
    • Xiao, B. et al. Structure of mammalian AMPK and its regulation by ADP. Nature 472, 230-233 (2011).
    • (2011) Nature , vol.472 , pp. 230-233
    • Xiao, B.1
  • 2
    • 78650606464 scopus 로고    scopus 로고
    • Beta-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK)
    • Oakhill, J. S. et al. beta-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK). Proc. Natl Acad. Sci. USA 107, 19237-19241 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19237-19241
    • Oakhill, J.S.1
  • 3
    • 84863719838 scopus 로고    scopus 로고
    • AMP-activated protein kinase undergoes nucleotide-dependent conformational changes
    • Chen, L. et al. AMP-activated protein kinase undergoes nucleotide-dependent conformational changes. Nat. Struct. Mol. Biol. 19, 716-718 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 716-718
    • Chen, L.1
  • 4
    • 79959338922 scopus 로고    scopus 로고
    • AMPK is a direct adenylate charge-regulated protein kinase
    • Oakhill, J. S. et al. AMPK is a direct adenylate charge-regulated protein kinase. Science 332, 1433-1435 (2011).
    • (2011) Science , vol.332 , pp. 1433-1435
    • Oakhill, J.S.1
  • 5
    • 84885168009 scopus 로고    scopus 로고
    • AMP is a true physiological regulator of AMP-activated protein kinase by both allosteric activation and enhancing net phosphorylation
    • Gowans, G. J., Hawley, S. A., Ross, F. A. & Hardie, D. G. AMP is a true physiological regulator of AMP-activated protein kinase by both allosteric activation and enhancing net phosphorylation. Cell Metab. 18, 556-566 (2013).
    • (2013) Cell Metab. , vol.18 , pp. 556-566
    • Gowans, G.J.1    Hawley, S.A.2    Ross, F.A.3    Hardie, D.G.4
  • 6
    • 84878971103 scopus 로고    scopus 로고
    • Conserved regulatory elements in AMPK
    • Chen, L. et al. Conserved regulatory elements in AMPK. Nature 498, E8-E10 (2013).
    • (2013) Nature , vol.498 , pp. E8-E10
    • Chen, L.1
  • 7
    • 84920276724 scopus 로고    scopus 로고
    • Structural basis of AMPK regulation by adenine nucleotides and glycogen
    • Li, X. et al. Structural basis of AMPK regulation by adenine nucleotides and glycogen. Cell Res. 25, 398 (2015).
    • (2015) Cell Res. , vol.25 , pp. 398
    • Li, X.1
  • 8
    • 84890963021 scopus 로고    scopus 로고
    • Structural basis of AMPK regulation by small molecule activators
    • Xiao, B. et al. Structural basis of AMPK regulation by small molecule activators. Nat. Commun. 4, 3017 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 3017
    • Xiao, B.1
  • 9
    • 84869837353 scopus 로고    scopus 로고
    • Direct AMP-activated protein kinase activators: A review of evidence from the patent literature
    • Giordanetto, F. & Karis, D. Direct AMP-activated protein kinase activators: a review of evidence from the patent literature. Expert Opin. Ther. Pat. 22, 1467-1477 (2012).
    • (2012) Expert Opin. Ther. Pat. , vol.22 , pp. 1467-1477
    • Giordanetto, F.1    Karis, D.2
  • 10
    • 84905719900 scopus 로고    scopus 로고
    • Structural basis for AMPK activation: Natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms
    • Calabrese, M. F. et al. Structural basis for AMPK activation: natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms. Structure. 22, 1161-1172 (2014).
    • (2014) Structure , vol.22 , pp. 1161-1172
    • Calabrese, M.F.1
  • 11
    • 84920287728 scopus 로고    scopus 로고
    • Choreography of AMPK activation
    • Langendorf, C. G. & Kemp, B. E. Choreography of AMPK activation. Cell Res. 25, 5-6 (2015).
    • (2015) Cell Res. , vol.25 , pp. 5-6
    • Langendorf, C.G.1    Kemp, B.E.2
  • 12
    • 84861222690 scopus 로고    scopus 로고
    • The ancient drug salicylate directly activates AMP-activated protein kinase
    • Hawley, S. A. et al. The ancient drug salicylate directly activates AMP-activated protein kinase. Science 336, 918-922 (2012).
    • (2012) Science , vol.336 , pp. 918-922
    • Hawley, S.A.1
  • 13
    • 84901329684 scopus 로고    scopus 로고
    • Small molecule drug A-769662 and AMP synergistically activate naive AMPK independent of upstream kinase signaling
    • Scott, J. W. et al. Small molecule drug A-769662 and AMP synergistically activate naive AMPK independent of upstream kinase signaling. Chem. Biol. 21, 619-627 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 619-627
    • Scott, J.W.1
  • 14
    • 36348978499 scopus 로고    scopus 로고
    • Defining the mechanism of activation of AMP-activated protein kinase by the small molecule A-769662, a member of the thienopyridone family
    • Sanders, M. J. et al. Defining the mechanism of activation of AMP-activated protein kinase by the small molecule A-769662, a member of the thienopyridone family. J. Biol. Chem. 282, 32539-32548 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 32539-32548
    • Sanders, M.J.1
  • 15
    • 78650224772 scopus 로고    scopus 로고
    • A potent and selective AMPK activator that inhibits de novo lipogenesis
    • Gomez-Galeno, J. E. et al. A potent and selective AMPK activator that inhibits de novo lipogenesis. ACS Med. Chem. Lett. 1, 478-482 (2010).
    • (2010) ACS Med. Chem. Lett. , vol.1 , pp. 478-482
    • Gomez-Galeno, J.E.1
  • 16
    • 84904556335 scopus 로고    scopus 로고
    • Mechanism of action of compound-13: An alpha1-selective small molecule activator of AMPK
    • Hunter, R. W. et al. Mechanism of action of compound-13: an alpha1-selective small molecule activator of AMPK. Chem. Biol. 21, 866-879 (2014).
    • (2014) Chem. Biol. , vol.21 , pp. 866-879
    • Hunter, R.W.1
  • 17
    • 84955464040 scopus 로고    scopus 로고
    • Differential regulation by AMP and ADP of AMPK complexes containing different gamma subunit isoforms
    • Ross, F., Jensen, T. E. & Hardie, D. G. Differential regulation by AMP and ADP of AMPK complexes containing different gamma subunit isoforms. Biochem. J. 473, 189-199 (2016).
    • (2016) Biochem. J. , vol.473 , pp. 189-199
    • Ross, F.1    Jensen, T.E.2    Hardie, D.G.3
  • 18
    • 4644309036 scopus 로고    scopus 로고
    • The 5′-AMP-activated protein kinase gamma3 isoform has a key role in carbohydrate and lipid metabolism in glycolytic skeletal muscle
    • Barnes, B. R. et al. The 5′-AMP-activated protein kinase gamma3 isoform has a key role in carbohydrate and lipid metabolism in glycolytic skeletal muscle. J. Biol. Chem. 279, 38441-38447 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 38441-38447
    • Barnes, B.R.1
  • 19
    • 77955420075 scopus 로고    scopus 로고
    • Escherichia coli expression, purification and characterization of functional full-length recombinant alpha2beta2gamma3 heterotrimeric complex of human AMP-activated protein kinase
    • Rajamohan, F. et al. Escherichia coli expression, purification and characterization of functional full-length recombinant alpha2beta2gamma3 heterotrimeric complex of human AMP-activated protein kinase. Protein Expr. Purif. 73, 189-197 (2010).
    • (2010) Protein Expr. Purif. , vol.73 , pp. 189-197
    • Rajamohan, F.1
  • 20
    • 75349091799 scopus 로고    scopus 로고
    • Defining the conserved internal architecture of a protein kinase
    • Kornev, A. P. & Taylor, S. S. Defining the conserved internal architecture of a protein kinase. Biochim. Biophys. Acta 1804, 440-444 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 440-444
    • Kornev, A.P.1    Taylor, S.S.2
  • 21
    • 0034141355 scopus 로고    scopus 로고
    • The regulation of AMP-activated protein kinase by phosphorylation
    • Stein, S. C., Woods, A., Jones, N. A., Davison, M. D. & Carling, D. The regulation of AMP-activated protein kinase by phosphorylation. Biochem. J. 345(Pt 3): 437-443 (2000).
    • (2000) Biochem. J. , vol.345 , pp. 437-443
    • Stein, S.C.1    Woods, A.2    Jones, N.A.3    Davison, M.D.4    Carling, D.5
  • 22
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 25
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 27
    • 77957946297 scopus 로고    scopus 로고
    • (Global Phasing Ltd., Cambridge, United Kingdom)
    • Bricogne, G. et al. BUSTER, Version 2.10.0 (Global Phasing Ltd., Cambridge, United Kingdom, 2011).
    • (2011) BUSTER, Version 2.10.0
    • Bricogne, G.1
  • 28
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W. & van Aalten, D. M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 60, 1355-1363 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 29
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J. & Wodak, S. J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55, 191-205 (1999).
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 30
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. D66, 12-21 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.D66 , pp. 12-21
    • Chen, V.B.1
  • 31
    • 84935013342 scopus 로고    scopus 로고
    • Inhibition of AMP-activated protein kinase at the allosteric drug-binding site promotes islet insulin release
    • Scott, J. W. et al. Inhibition of AMP-activated protein kinase at the allosteric drug-binding site promotes islet insulin release. Chem. Biol. 22, 705-711 (2015).
    • (2015) Chem. Biol. , vol.22 , pp. 705-711
    • Scott, J.W.1
  • 32
    • 56049112796 scopus 로고    scopus 로고
    • Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes
    • Scott, J. W. et al. Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes. Chem. Biol. 15, 1220-1230 (2008).
    • (2008) Chem. Biol. , vol.15 , pp. 1220-1230
    • Scott, J.W.1
  • 33
    • 0018174535 scopus 로고
    • Isolation of phosphorylated peptides and proteins on ion exchange papers
    • Glass, D. B., Masaracchia, R. A., Feramisco, J. R. & Kemp, B. E. Isolation of phosphorylated peptides and proteins on ion exchange papers. Anal. Biochem. 87, 566-575 (1978).
    • (1978) Anal. Biochem. , vol.87 , pp. 566-575
    • Glass, D.B.1    Masaracchia, R.A.2    Feramisco, J.R.3    Kemp, B.E.4


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