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Volumn 18, Issue 4, 2013, Pages 556-566

AMP is a true physiological regulator of amp-activated protein kinase by both allosteric activation and enhancing net phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

6,7 DIHYDRO 4 HYDROXY 3 (2' HYDROXY 1,1' BIPHENYL 4 YL) 6 OXOTHIENO[2,3 B]PYRIDINE 5 CARBONITRILE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; BERBERINE; CALCIMYCIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; MAGNESIUM CHLORIDE;

EID: 84885168009     PISSN: 15504131     EISSN: 19327420     Source Type: Journal    
DOI: 10.1016/j.cmet.2013.08.019     Document Type: Article
Times cited : (406)

References (41)
  • 1
    • 34848843526 scopus 로고    scopus 로고
    • Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1
    • Amodeo, G.A., Rudolph, M.J., and Tong, L. (2007). Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1. Nature 449, 492-495.
    • (2007) Nature , vol.449 , pp. 492-495
    • Amodeo, G.A.1    Rudolph, M.J.2    Tong, L.3
  • 2
    • 0023642627 scopus 로고
    • A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis
    • Carling, D., Zammit, V.A., and Hardie, D.G. (1987). A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis. FEBS Lett. 223, 217-222.
    • (1987) FEBS Lett. , vol.223 , pp. 217-222
    • Carling, D.1    Zammit, V.A.2    Hardie, D.G.3
  • 3
    • 0024786438 scopus 로고
    • Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl- CoA reductase kinase activities
    • Carling, D., Clarke, P.R., Zammit, V.A., and Hardie, D.G. (1989). Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl- CoA reductase kinase activities. Eur. J. Biochem. 186, 129-136.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 129-136
    • Carling, D.1    Clarke, P.R.2    Zammit, V.A.3    Hardie, D.G.4
  • 4
    • 84862493914 scopus 로고    scopus 로고
    • AMP-activated protein kinase: New regulation, new roles?
    • Carling, D., Thornton, C., Woods, A., and Sanders, M.J. (2012). AMP-activated protein kinase: new regulation, new roles? Biochem. J. 445, 11-27.
    • (2012) Biochem. J. , vol.445 , pp. 11-27
    • Carling, D.1    Thornton, C.2    Woods, A.3    Sanders, M.J.4
  • 6
    • 0029561919 scopus 로고
    • 50-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C alpha and native bovine protein phosphatase-2AC
    • Davies, S.P., Helps, N.R., Cohen, P.T.W., and Hardie, D.G. (1995). 50-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2C alpha and native bovine protein phosphatase-2AC. FEBS Lett. 377, 421-425.
    • (1995) FEBS Lett. , vol.377 , pp. 421-425
    • Davies, S.P.1    Helps, N.R.2    Cohen, P.T.W.3    Hardie, D.G.4
  • 9
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase: The energy charge hypothesis revisited
    • Hardie, D.G., and Hawley, S.A. (2001). AMP-activated protein kinase: the energy charge hypothesis revisited. Bioessays 23, 1112-1119.
    • (2001) Bioessays , vol.23 , pp. 1112-1119
    • Hardie, D.G.1    Hawley, S.A.2
  • 10
    • 0033648637 scopus 로고    scopus 로고
    • Analysis of the role of the AMPactivated protein kinase in the response to cellular stress
    • Hardie, D.G., Salt, I.P., and Davies, S.P. (2000). Analysis of the role of the AMPactivated protein kinase in the response to cellular stress. Methods Mol. Biol. 99, 63-74.
    • (2000) Methods Mol. Biol. , vol.99 , pp. 63-74
    • Hardie, D.G.1    Salt, I.P.2    Davies, S.P.3
  • 11
    • 80052385397 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Also regulated by ADP? Trends Biochem
    • Hardie, D.G., Carling, D., and Gamblin, S.J. (2011). AMP-activated protein kinase: also regulated by ADP? Trends Biochem. Sci. 36, 470-477.
    • (2011) Sci. , vol.36 , pp. 470-477
    • Hardie, D.G.1    Carling, D.2    Gamblin, S.J.3
  • 12
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • Hardie, D.G., Ross, F.A., and Hawley, S.A. (2012). AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nat. Rev. Mol. Cell Biol. 13, 251-262.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 13
    • 0028845251 scopus 로고
    • 50-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase i cascade, via three independent mechanisms
    • Hawley, S.A., Selbert, M.A., Goldstein, E.G., Edelman, A.M., Carling, D., and Hardie, D.G. (1995). 50-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J. Biol. Chem. 270, 27186-27191.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27186-27191
    • Hawley, S.A.1    Selbert, M.A.2    Goldstein, E.G.3    Edelman, A.M.4    Carling, D.5    Hardie, D.G.6
  • 14
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
    • Hawley, S.A., Davison, M., Woods, A., Davies, S.P., Beri, R.K., Carling, D., and Hardie, D.G. (1996). Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J. Biol. Chem. 271, 27879-27887.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 15
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade
    • Hawley, S.A., Boudeau, J., Reid, J.L., Mustard, K.J., Udd, L., Mäkelä, T.P., Alessi, D.R., and Hardie, D.G. (2003). Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade. J. Biol. 2, 28.
    • (2003) J. Biol. , vol.2 , pp. 28
    • Hawley, S.A.1    Boudeau, J.2    Reid, J.L.3    Mustard, K.J.4    Udd, L.5    Mäkelä, T.P.6    Alessi, D.R.7    Hardie, D.G.8
  • 16
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase
    • Hawley, S.A., Pan, D.A., Mustard, K.J., Ross, L., Bain, J., Edelman, A.M., Frenguelli, B.G., and Hardie, D.G. (2005). Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Cell Metab. 2, 9-19.
    • (2005) Cell Metab. , vol.2 , pp. 9-19
    • Hawley, S.A.1    Pan, D.A.2    Mustard, K.J.3    Ross, L.4    Bain, J.5    Edelman, A.M.6    Frenguelli, B.G.7    Hardie, D.G.8
  • 19
    • 23844471263 scopus 로고    scopus 로고
    • The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases
    • Hurley, R.L., Anderson, K.A., Franzone, J.M., Kemp, B.E., Means, A.R., and Witters, L.A. (2005). The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases. J. Biol. Chem. 280, 29060-29066.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29060-29066
    • Hurley, R.L.1    Anderson, K.A.2    Franzone, J.M.3    Kemp, B.E.4    Means, A.R.5    Witters, L.A.6
  • 20
    • 70349449239 scopus 로고    scopus 로고
    • Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators
    • Imamura, H., Nhat, K.P., Togawa, H., Saito, K., Iino, R., Kato-Yamada, Y., Nagai, T., and Noji, H. (2009). Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators. Proc. Natl. Acad. Sci. USA 106, 15651-15656.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 15651-15656
    • Imamura, H.1    Nhat, K.P.2    Togawa, H.3    Saito, K.4    Iino, R.5    Kato-Yamada, Y.6    Nagai, T.7    Noji, H.8
  • 21
    • 35148850705 scopus 로고    scopus 로고
    • Structural insight into AMPK regulation: ADP comes into play
    • Jin, X., Townley, R., and Shapiro, L. (2007). Structural insight into AMPK regulation: ADP comes into play. Structure 15, 1285-1295.
    • (2007) Structure , vol.15 , pp. 1285-1295
    • Jin, X.1    Townley, R.2    Shapiro, L.3
  • 22
    • 35148867829 scopus 로고    scopus 로고
    • AMPK structure and regulation from three angles
    • Kemp, B.E., Oakhill, J.S., and Scott, J.W. (2007). AMPK structure and regulation from three angles. Structure 15, 1161-1163.
    • (2007) Structure , vol.15 , pp. 1161-1163
    • Kemp, B.E.1    Oakhill, J.S.2    Scott, J.W.3
  • 23
    • 33745840203 scopus 로고    scopus 로고
    • 50-AMP-activated protein kinase (AMPK) is induced by low-oxygen and glucose deprivation conditions found in solidtumor microenvironments
    • Laderoute, K.R., Amin, K., Calaoagan, J.M., Knapp, M., Le, T., Orduna, J., Foretz, M., and Viollet, B. (2006). 50-AMP-activated protein kinase (AMPK) is induced by low-oxygen and glucose deprivation conditions found in solidtumor microenvironments. Mol. Cell. Biol. 26, 5336-5347.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5336-5347
    • Laderoute, K.R.1    Amin, K.2    Calaoagan, J.M.3    Knapp, M.4    Le, T.5    Orduna, J.6    Foretz, M.7    Viollet, B.8
  • 24
    • 0018696222 scopus 로고
    • Effects of pH and free Mg2+ on the Keq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions
    • Lawson, J.W., and Veech, R.L. (1979). Effects of pH and free Mg2+ on the Keq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions. J. Biol. Chem. 254, 6528-6537.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6528-6537
    • Lawson, J.W.1    Veech, R.L.2
  • 26
    • 0043071497 scopus 로고    scopus 로고
    • Mammalian AMP-activated protein kinase: Functional, heterotrimeric complexes by co-expression of subunits in Escherichia coli
    • Neumann, D., Woods, A., Carling, D., Wallimann, T., and Schlattner, U. (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    Woods, A.2    Carling, D.3    Wallimann, T.4    Schlattner, U.5
  • 27
    • 78650606464 scopus 로고    scopus 로고
    • B-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK)
    • Oakhill, J.S., Chen, Z.P., Scott, J.W., Steel, R., Castelli, L.A., Ling, N., Macaulay, S.L., and Kemp, B.E. (2010). b-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) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 19237-19241
    • Oakhill, J.S.1    Chen, Z.P.2    Scott, J.W.3    Steel, R.4    Castelli, L.A.5    Ling, N.6    Macaulay, S.L.7    Kemp, B.E.8
  • 29
    • 84857687439 scopus 로고    scopus 로고
    • AMPK functions as an adenylate charge-regulated protein kinase
    • Oakhill, J.S., Scott, J.W., and Kemp, B.E. (2012). AMPK functions as an adenylate charge-regulated protein kinase. Trends Endocrinol. Metab. 23, 125-132.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 125-132
    • Oakhill, J.S.1    Scott, J.W.2    Kemp, B.E.3
  • 31
    • 17144474893 scopus 로고    scopus 로고
    • Activity of LKB1 and AMPK-related kinases in skeletal muscle: Effects of contraction, phenformin, and AICAR
    • Sakamoto, K., Göransson, O., Hardie, D.G., and Alessi, D.R. (2004). Activity of LKB1 and AMPK-related kinases in skeletal muscle: effects of contraction, phenformin, and AICAR. Am. J. Physiol. Endocrinol. Metab. 287, E310-E317.
    • (2004) Am. J. Physiol. Endocrinol. Metab. , vol.287
    • Sakamoto, K.1    Göransson, O.2    Hardie, D.G.3    Alessi, D.R.4
  • 32
    • 34147152841 scopus 로고    scopus 로고
    • Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    • Sanders, M.J., Grondin, P.O., Hegarty, B.D., Snowden, M.A., and Carling, D. (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    Grondin, P.O.2    Hegarty, B.D.3    Snowden, M.A.4    Carling, D.5
  • 34
    • 1542618348 scopus 로고    scopus 로고
    • The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress
    • Shaw, R.J., Kosmatka, M., Bardeesy, N., Hurley, R.L., Witters, L.A., DePinho, R.A., and Cantley, L.C. (2004). The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress. Proc. Natl. Acad. Sci. USA 101, 3329-3335.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3329-3335
    • Shaw, R.J.1    Kosmatka, M.2    Bardeesy, N.3    Hurley, R.L.4    Witters, L.A.5    Depinho, R.A.6    Cantley, L.C.7
  • 35
    • 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., and Carling, D. (2000). The regulation of AMP-activated protein kinase by phosphorylation. Biochem. J. 345, 437-443.
    • (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
  • 36
    • 33845949733 scopus 로고    scopus 로고
    • Dissecting the role of 50-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase
    • Suter, M., Riek, U., Tuerk, R., Schlattner, U., Wallimann, T., and Neumann, D. (2006). Dissecting the role of 50-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase. J. Biol. Chem. 281, 32207-32216.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32207-32216
    • Suter, M.1    Riek, U.2    Tuerk, R.3    Schlattner, U.4    Wallimann, T.5    Neumann, D.6
  • 37
    • 34047161436 scopus 로고    scopus 로고
    • Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase
    • Townley, R., and Shapiro, L. (2007). Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase. Science 315, 1726-1729.
    • (2007) Science , vol.315 , pp. 1726-1729
    • Townley, R.1    Shapiro, L.2
  • 39
    • 23044437445 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells
    • Woods, A., Dickerson, K., Heath, R., Hong, S.P., Momcilovic, M., Johnstone, S.R., Carlson, M., and Carling, D. (2005). Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells. Cell Metab. 2, 21-33.
    • (2005) Cell Metab. , vol.2 , pp. 21-33
    • Woods, A.1    Dickerson, K.2    Heath, R.3    Hong, S.P.4    Momcilovic, M.5    Johnstone, S.R.6    Carlson, M.7    Carling, D.8


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