메뉴 건너뛰기




Volumn 5, Issue MAY, 2014, Pages

Mechanisms of regulation of SNF1/AMPK/SnRK1 protein kinases

Author keywords

AMPK; Arabidopsis; Energy signaling; Kinase regulation; SNF1; SnRK1; Stress

Indexed keywords


EID: 84902259326     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2014.00190     Document Type: Review
Times cited : (194)

References (196)
  • 1
    • 0025936416 scopus 로고
    • Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA
    • doi: 10.1073/pnas.88.19.8602
    • Alderson, A., Sabelli, P. A., Dickinson, J. R., Cole, D., Richardson, M., Kreis, M., et al. (1991). Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA. Proc. Natl. Acad. Sci. U.S.A. 88, 8602-8605. doi: 10.1073/pnas.88.19.8602
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8602-8605
    • Alderson, A.1    Sabelli, P.A.2    Dickinson, J.R.3    Cole, D.4    Richardson, M.5    Kreis, M.6
  • 2
    • 33746353046 scopus 로고    scopus 로고
    • LKB1-dependent signaling pathways
    • doi: 10.1146/annurev.biochem.75.103004.142702
    • Alessi, D. R., Sakamoto, K., and Bayascas, J. R. (2006). LKB1-dependent signaling pathways. Annu. Rev. Biochem.75, 137-163. doi: 10.1146/annurev.biochem.75.103004.142702
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 137-163
    • Alessi, D.R.1    Sakamoto, K.2    Bayascas, J.R.3
  • 3
    • 42449090346 scopus 로고    scopus 로고
    • Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains
    • doi: 10.1042/BJ20080067
    • Al-Hakim, A. K., Zagorska, A., Chapman, L., Deak, M., Peggie, M., and Alessi, D. R. (2008). Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains. Biochem. J. 411, 249-260. doi: 10.1042/BJ20080067
    • (2008) Biochem. J. , vol.411 , pp. 249-260
    • Al-Hakim, A.K.1    Zagorska, A.2    Chapman, L.3    Deak, M.4    Peggie, M.5    Alessi, D.R.6
  • 4
    • 34848843526 scopus 로고    scopus 로고
    • Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1
    • doi: 10.1038/nature06127
    • 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. doi: 10.1038/nature06127
    • (2007) Nature , vol.449 , pp. 492-495
    • Amodeo, G.A.1    Rudolph, M.J.2    Tong, L.3
  • 5
    • 57749085445 scopus 로고    scopus 로고
    • Interaction of the WD40 domain of a myoinositol polyphosphate 5-phosphatase with SnRK1 links inositol, sugar, and stress signaling
    • doi: 10.1104/pp.108.130575
    • Ananieva, E. A., Gillaspy, G. E., Ely, A., Burnette, R. N., and Erickson, F. L. (2008). Interaction of the WD40 domain of a myoinositol polyphosphate 5-phosphatase with SnRK1 links inositol, sugar, and stress signaling. Plant Physiol.148, 1868-1882. doi: 10.1104/pp.108.130575
    • (2008) Plant Physiol. , vol.148 , pp. 1868-1882
    • Ananieva, E.A.1    Gillaspy, G.E.2    Ely, A.3    Burnette, R.N.4    Erickson, F.L.5
  • 6
    • 42649105456 scopus 로고    scopus 로고
    • Hypothalamic CaMKK2 contributes to the regulation of energy balance
    • doi: 10.1016/j.cmet.2008.02.011
    • Anderson, K. A., Ribar, T. J., Lin, F., Noeldner, P. K., Green, M. F., Muehlbauer, M. J., et al. (2008). Hypothalamic CaMKK2 contributes to the regulation of energy balance. Cell Metab. 7, 377-388. doi: 10.1016/j.cmet.2008.02.011
    • (2008) Cell Metab. , vol.7 , pp. 377-388
    • Anderson, K.A.1    Ribar, T.J.2    Lin, F.3    Noeldner, P.K.4    Green, M.F.5    Muehlbauer, M.J.6
  • 7
    • 0032476052 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase
    • doi: 10.1074/jbc.273.40.25864
    • Ashrafi, K., Farazi, T. A., and Gordon, J. I. (1998). A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase. J. Biol. Chem. 273, 25864-25874. doi: 10.1074/jbc.273.40.25864
    • (1998) J. Biol. Chem. , vol.273 , pp. 25864-25874
    • Ashrafi, K.1    Farazi, T.A.2    Gordon, J.I.3
  • 8
    • 84863675258 scopus 로고    scopus 로고
    • The beta-subunit of the SnRK1 complex is phosphorylated by the plant cell death suppressor Adi3
    • doi: 10.1104/pp.112.198432
    • Avila, J., Gregory, O. G., Su, D., Deeter, T. A., Chen, S., Silva-Sanchez, C., et al. (2012). The beta-subunit of the SnRK1 complex is phosphorylated by the plant cell death suppressor Adi3. Plant Physiol. 159, 1277-1290. doi: 10.1104/pp.112.198432
    • (2012) Plant Physiol. , vol.159 , pp. 1277-1290
    • Avila, J.1    Gregory, O.G.2    Su, D.3    Deeter, T.A.4    Chen, S.5    Silva-Sanchez, C.6
  • 9
    • 34548190012 scopus 로고    scopus 로고
    • A central integrator of transcription networks in plant stress and energy signalling
    • doi: 10.1038/nature06069
    • Baena-Gonzalez, E., Rolland, F., Thevelein, J. M., and Sheen, J. (2007). A central integrator of transcription networks in plant stress and energy signalling. Nature 448, 938-942. doi: 10.1038/nature06069
    • (2007) Nature , vol.448 , pp. 938-942
    • Baena-Gonzalez, E.1    Rolland, F.2    Thevelein, J.M.3    Sheen, J.4
  • 10
    • 50349090461 scopus 로고    scopus 로고
    • Convergent energy and stress signaling
    • doi: 10.1016/j.tplants.2008.06.006
    • Baena-Gonzalez, E., and Sheen, J. (2008). Convergent energy and stress signaling. Trends Plant Sci. 13, 474-482. doi: 10.1016/j.tplants.2008.06.006
    • (2008) Trends Plant Sci. , vol.13 , pp. 474-482
    • Baena-Gonzalez, E.1    Sheen, J.2
  • 11
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • doi: 10.1016/S0968-0004(96)30046-7
    • Bateman, A. (1997). The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem. Sci. 22, 12-13. doi: 10.1016/S0968-0004(96)30046-7
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 12-13
    • Bateman, A.1
  • 12
    • 33751072349 scopus 로고    scopus 로고
    • Resveratrol improves health and survival of mice on a high-calorie diet
    • doi: 10.1038/nature05354
    • Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., et al. (2006). Resveratrol improves health and survival of mice on a high-calorie diet. Nature 444, 337-342. doi: 10.1038/nature05354
    • (2006) Nature , vol.444 , pp. 337-342
    • Baur, J.A.1    Pearson, K.J.2    Price, N.L.3    Jamieson, H.A.4    Lerin, C.5    Kalra, A.6
  • 13
    • 0033609163 scopus 로고    scopus 로고
    • Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like protein kinases
    • doi: 10.1073/pnas.96.9.5322
    • Bhalerao, R. P., Salchert, K., Bako, L., Okresz, L., Szabados, L., Muranaka, T., et al. (1999). Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like protein kinases. Proc. Natl. Acad. Sci. U.S.A. 96, 5322-5327. doi: 10.1073/pnas.96.9.5322
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 5322-5327
    • Bhalerao, R.P.1    Salchert, K.2    Bako, L.3    Okresz, L.4    Szabados, L.5    Muranaka, T.6
  • 14
    • 0028040192 scopus 로고
    • Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae
    • Cannon, J. F., Pringle, J. R., Fiechter, A., and Khalil, M. (1994). Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae. Genetics 136, 485-503.
    • (1994) Genetics , vol.136 , pp. 485-503
    • Cannon, J.F.1    Pringle, J.R.2    Fiechter, A.3    Khalil, M.4
  • 15
    • 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
    • doi: 10.1111/j.1432-1033.1989.tb15186.x
    • 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. doi: 10.1111/j.1432-1033.1989.tb15186.x
    • (1989) Eur. J. Biochem. , vol.186 , pp. 129-136
    • Carling, D.1    Clarke, P.R.2    Zammit, V.A.3    Hardie, D.G.4
  • 16
    • 84862493914 scopus 로고    scopus 로고
    • AMP-activated protein kinase: New regulation, new roles?
    • doi: 10.1042/BJ20120546
    • Carling, D., Thornton, C., Woods, A., and Sanders, M. J. (2012). AMP-activated protein kinase: new regulation, new roles? Biochem. J. 445, 11-27. doi: 10.1042/BJ20120546
    • (2012) Biochem. J. , vol.445 , pp. 11-27
    • Carling, D.1    Thornton, C.2    Woods, A.3    Sanders, M.J.4
  • 17
    • 0023642627 scopus 로고
    • A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis
    • doi: 10.1016/0014-5793(87)80292-2
    • 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. doi: 10.1016/0014-5793(87)80292-2
    • (1987) FEBS Lett. , vol.223 , pp. 217-222
    • Carling, D.1    Zammit, V.A.2    Hardie, D.G.3
  • 18
    • 84861840057 scopus 로고    scopus 로고
    • Glucose-induced posttranslational activation of protein phosphatases PP2A and PP1 in yeast
    • doi: 10.1038/cr.2012.20
    • Castermans, D., Somers, I., Kriel, J., Louwet, W., Wera, S., Versele, M., et al. (2012). Glucose-induced posttranslational activation of protein phosphatases PP2A and PP1 in yeast. Cell Res. 22, 1058-1077. doi: 10.1038/cr.2012.20
    • (2012) Cell Res. , vol.22 , pp. 1058-1077
    • Castermans, D.1    Somers, I.2    Kriel, J.3    Louwet, W.4    Wera, S.5    Versele, M.6
  • 19
    • 84866368760 scopus 로고    scopus 로고
    • SUMO, a heavyweight player in plant abiotic stress responses
    • doi: 10.1007/s00018-012-1094-2
    • Castro, P. H., Tavares, R. M., Bejarano, E. R., and Azevedo, H. (2012). SUMO, a heavyweight player in plant abiotic stress responses. Cell. Mol. Life Sci. 69, 3269-3283. doi: 10.1007/s00018-012-1094-2
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 3269-3283
    • Castro, P.H.1    Tavares, R.M.2    Bejarano, E.R.3    Azevedo, H.4
  • 20
    • 44649085556 scopus 로고    scopus 로고
    • Citrate diminishes hypothalamic acetyl-CoA carboxylase phosphorylation and modulates satiety signals and hepatic mechanisms involved in glucose homeostasis in rats
    • doi: 10.1016/j.lfs.2008.04.015
    • Cesquini, M., Stoppa, G. R., Prada, P. O., Torsoni, A. S., Romanatto, T., Souza, A., et al. (2008). Citrate diminishes hypothalamic acetyl-CoA carboxylase phosphorylation and modulates satiety signals and hepatic mechanisms involved in glucose homeostasis in rats. Life Sci. 82, 1262-1271. doi: 10.1016/j.lfs.2008.04.015
    • (2008) Life Sci. , vol.82 , pp. 1262-1271
    • Cesquini, M.1    Stoppa, G.R.2    Prada, P.O.3    Torsoni, A.S.4    Romanatto, T.5    Souza, A.6
  • 21
    • 84455161597 scopus 로고    scopus 로고
    • Subunit and domain requirements for adenylate-mediated protection of Snf1 kinase activation loop from dephosphorylation
    • doi: 10.1074/jbc.M111.315895
    • Chandrashekarappa, D. G., Mccartney, R. R., and Schmidt, M. C. (2011). Subunit and domain requirements for adenylate-mediated protection of Snf1 kinase activation loop from dephosphorylation. J. Biol. Chem. 286, 44532-44541. doi: 10.1074/jbc.M111.315895
    • (2011) J. Biol. Chem. , vol.286 , pp. 44532-44541
    • Chandrashekarappa, D.G.1    Mccartney, R.R.2    Schmidt, M.C.3
  • 22
    • 84872079812 scopus 로고    scopus 로고
    • Ligand binding to the AMP-activated protein kinase active site mediates protection of the activation loop from dephosphorylation
    • doi: 10.1074/jbc.M112.422659
    • Chandrashekarappa, D. G., Mccartney, R. R., and Schmidt, M. C. (2013). Ligand binding to the AMP-activated protein kinase active site mediates protection of the activation loop from dephosphorylation. J. Biol. Chem. 288, 89-98. doi: 10.1074/jbc.M112.422659
    • (2013) J. Biol. Chem. , vol.288 , pp. 89-98
    • Chandrashekarappa, D.G.1    Mccartney, R.R.2    Schmidt, M.C.3
  • 23
    • 67649484365 scopus 로고    scopus 로고
    • Structural insight into the autoinhibition mechanism of AMP-activated protein kinase
    • doi: 10.1038/nature08075
    • Chen, L., Jiao, Z. H., Zheng, L. S., Zhang, Y. Y., Xie, S. T., Wang, Z. X., et al. (2009). Structural insight into the autoinhibition mechanism of AMP-activated protein kinase. Nature 459, 1146-1149. doi: 10.1038/nature08075
    • (2009) Nature , vol.459 , pp. 1146-1149
    • Chen, L.1    Jiao, Z.H.2    Zheng, L.S.3    Zhang, Y.Y.4    Xie, S.T.5    Wang, Z.X.6
  • 24
    • 84875672536 scopus 로고    scopus 로고
    • TAK1 activates AMPK-dependent cell death pathway in hydrogen peroxide-treated cardiomyocytes, inhibited by heat shock protein-70
    • doi: 10.1007/s11010-013-1568-z
    • Chen, Z., Shen, X., Shen, F., Zhong, W., Wu, H., Liu, S., et al. (2013). TAK1 activates AMPK-dependent cell death pathway in hydrogen peroxide-treated cardiomyocytes, inhibited by heat shock protein-70. Mol. Cell. Biochem.377, 35-44. doi: 10.1007/s11010-013-1568-z
    • (2013) Mol. Cell. Biochem. , vol.377 , pp. 35-44
    • Chen, Z.1    Shen, X.2    Shen, F.3    Zhong, W.4    Wu, H.5    Liu, S.6
  • 25
    • 84855865473 scopus 로고    scopus 로고
    • Evidence that abscisic acid promotes degradation of SNF1-related protein kinase (SnRK) 1 in wheat and activation of a putative calcium-dependent SnRK2
    • doi: 10.1093/jxb/err320
    • Coello, P., Hirano, E., Hey, S. J., Muttucumaru, N., Martinez-Barajas, E., Parry, M. A., et al. (2012). Evidence that abscisic acid promotes degradation of SNF1-related protein kinase (SnRK) 1 in wheat and activation of a putative calcium-dependent SnRK2. J. Exp. Bot. 63, 913-924. doi: 10.1093/jxb/err320
    • (2012) J. Exp. Bot. , vol.63 , pp. 913-924
    • Coello, P.1    Hirano, E.2    Hey, S.J.3    Muttucumaru, N.4    Martinez-Barajas, E.5    Parry, M.A.6
  • 26
    • 85047689953 scopus 로고
    • 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells?
    • doi: 10.1111/j.1432-1033.1995.tb20498.x
    • Corton, J. M., Gillespie, J. G., Hawley, S. A., and Hardie, D. G. (1995). 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells? Eur. J. Biochem. 229, 558-565. doi: 10.1111/j.1432-1033.1995.tb20498.x
    • (1995) Eur. J. Biochem. , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 27
    • 77951213904 scopus 로고    scopus 로고
    • Cross-phosphorylation between Arabidopsis thaliana sucrose nonfermenting 1-related protein kinase 1 (AtSnRK1) and its activating kinase (AtSnAK) determines their catalytic activities
    • doi: 10.1074/jbc.M109.079194
    • Crozet, P., Jammes, F., Valot, B., Ambard-Bretteville, F., Nessler, S., Hodges, M., et al. (2010). Cross-phosphorylation between Arabidopsis thaliana sucrose nonfermenting 1-related protein kinase 1 (AtSnRK1) and its activating kinase (AtSnAK) determines their catalytic activities. J. Biol. Chem. 285, 12071-12077. doi: 10.1074/jbc.M109.079194
    • (2010) J. Biol. Chem. , vol.285 , pp. 12071-12077
    • Crozet, P.1    Jammes, F.2    Valot, B.3    Ambard-Bretteville, F.4    Nessler, S.5    Hodges, M.6
  • 28
    • 77952511548 scopus 로고    scopus 로고
    • Abscisic acid: Emergence of a core signaling network
    • doi: 10.1146/annurev-arplant-042809-112122
    • Cutler, S. R., Rodriguez, P. L., Finkelstein, R. R., and Abrams, S. R. (2010). Abscisic acid: emergence of a core signaling network. Annu. Rev. Plant Biol. 61, 651-679. doi: 10.1146/annurev-arplant-042809-112122
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 651-679
    • Cutler, S.R.1    Rodriguez, P.L.2    Finkelstein, R.R.3    Abrams, S.R.4
  • 29
    • 0029561919 scopus 로고
    • 5′-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
    • doi: 10.1016/0014-5793(95)01368-7
    • Davies, S. P., Helps, N. R., Cohen, P. T., and Hardie, D. G. (1995). 5′-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. doi: 10.1016/0014-5793(95)01368-7
    • (1995) FEBS Lett. , vol.377 , pp. 421-425
    • Davies, S.P.1    Helps, N.R.2    Cohen, P.T.3    Hardie, D.G.4
  • 30
    • 34247520659 scopus 로고    scopus 로고
    • Structure of a CBS-domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP and ZMP
    • doi: 10.1107/S0907444907009110
    • Day, P., Sharff, A., Parra, L., Cleasby, A., Williams, M., Horer, S., et al. (2007). Structure of a CBS-domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP and ZMP. Acta Crystallogr. D Biol. Crystallogr. 63, 587-596. doi: 10.1107/S0907444907009110
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 587-596
    • Day, P.1    Sharff, A.2    Parra, L.3    Cleasby, A.4    Williams, M.5    Horer, S.6
  • 31
    • 79961238547 scopus 로고    scopus 로고
    • Altering trehalose-6-phosphate content in transgenic potato tubers affects tuber growth and alters responsiveness to hormones during sprouting
    • doi: 10.1104/pp.111.179903
    • Debast, S., Nunes-Nesi, A., Hajirezaei, M. R., Hofmann, J., Sonnewald, U., Fernie, A. R., et al. (2011). Altering trehalose-6-phosphate content in transgenic potato tubers affects tuber growth and alters responsiveness to hormones during sprouting. Plant Physiol. 156, 1754-1771. doi: 10.1104/pp.111.179903
    • (2011) Plant Physiol. , vol.156 , pp. 1754-1771
    • Debast, S.1    Nunes-Nesi, A.2    Hajirezaei, M.R.3    Hofmann, J.4    Sonnewald, U.5    Fernie, A.R.6
  • 32
    • 80052425168 scopus 로고    scopus 로고
    • Growth arrest by trehalose-6-phosphate: An astonishing case of primary metabolite control over growth by way of the SnRK1 signaling pathway
    • doi: 10.1104/pp.111.180422
    • Delatte, T. L., Sedijani, P., Kondou, Y., Matsui, M., De Jong, G. J., Somsen, G. W., et al. (2011). Growth arrest by trehalose-6-phosphate: an astonishing case of primary metabolite control over growth by way of the SnRK1 signaling pathway. Plant Physiol. 157, 160-174. doi: 10.1104/pp.111.180422
    • (2011) Plant Physiol. , vol.157 , pp. 160-174
    • Delatte, T.L.1    Sedijani, P.2    Kondou, Y.3    Matsui, M.4    De Jong, G.J.5    Somsen, G.W.6
  • 33
    • 75049085233 scopus 로고    scopus 로고
    • PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis
    • doi: 10.1038/emboj.2009.339
    • Djouder, N., Tuerk, R. D., Suter, M., Salvioni, P., Thali, R. F., Scholz, R., et al. (2009). PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis. EMBO J. 29, 469-481. doi: 10.1038/emboj.2009.339
    • (2009) EMBO J. , vol.29 , pp. 469-481
    • Djouder, N.1    Tuerk, R.D.2    Suter, M.3    Salvioni, P.4    Thali, R.F.5    Scholz, R.6
  • 34
  • 35
    • 0036007980 scopus 로고    scopus 로고
    • Trehalose-6-phosphate synthase 1, which catalyses the first step in trehalose synthesis, is essential for Arabidopsis embryo maturation
    • doi: 10.1046/j.1365-313x.2002.01220.x
    • Eastmond, P. J., Van Dijken, A. J., Spielman, M., Kerr, A., Tissier, A. F., Dickinson, H. G., et al. (2002). Trehalose-6-phosphate synthase 1, which catalyses the first step in trehalose synthesis, is essential for Arabidopsis embryo maturation. Plant J. 29, 225-235. doi: 10.1046/j.1365-313x.2002.01220.x
    • (2002) Plant J. , vol.29 , pp. 225-235
    • Eastmond, P.J.1    Van Dijken, A.J.2    Spielman, M.3    Kerr, A.4    Tissier, A.F.5    Dickinson, H.G.6
  • 36
    • 31544468889 scopus 로고    scopus 로고
    • Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae
    • doi: 10.1042/BJ20051213
    • Elbing, K., Mccartney, R. R., and Schmidt, M. C. (2006a). Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae. Biochem. J. 393, 797-805. doi: 10.1042/BJ20051213
    • (2006) Biochem. J. , vol.393 , pp. 797-805
    • Elbing, K.1    Mccartney, R.R.2    Schmidt, M.C.3
  • 37
    • 33748744959 scopus 로고    scopus 로고
    • Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity
    • doi: 10.1074/jbc.M603811200
    • Elbing, K., Rubenstein, E. M., Mccartney, R. R., and Schmidt, M. C. (2006b). Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity. J. Biol. Chem. 281, 26170-26180. doi: 10.1074/jbc.M603811200
    • (2006) J. Biol. Chem. , vol.281 , pp. 26170-26180
    • Elbing, K.1    Rubenstein, E.M.2    Mccartney, R.R.3    Schmidt, M.C.4
  • 38
    • 78049234670 scopus 로고    scopus 로고
    • Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes
    • doi: 10.1073/pnas.1005452107
    • Elrouby, N., and Coupland, G. (2010). Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates identify Arabidopsis proteins implicated in diverse biological processes. Proc. Natl. Acad. Sci. U.S.A. 107, 17415-17420. doi: 10.1073/pnas.1005452107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17415-17420
    • Elrouby, N.1    Coupland, G.2
  • 39
    • 17944366393 scopus 로고    scopus 로고
    • SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase
    • doi: 10.1093/emboj/20.11.2742
    • Farras, R., Ferrando, A., Jasik, J., Kleinow, T., Okresz, L., Tiburcio, A., et al. (2001). SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase. EMBO J. 20, 2742-2756. doi: 10.1093/emboj/20.11.2742
    • (2001) EMBO J. , vol.20 , pp. 2742-2756
    • Farras, R.1    Ferrando, A.2    Jasik, J.3    Kleinow, T.4    Okresz, L.5    Tiburcio, A.6
  • 40
    • 76549120323 scopus 로고    scopus 로고
    • Pleiotropic regulatory locus 1 (PRL1) integrates the regulation of sugar responses with isoprenoid metabolism in Arabidopsis
    • doi: 10.1093/mp/ssp100
    • Flores-Perez, U., Perez-Gil, J., Closa, M., Wright, L. P., Botella-Pavia, P., Phillips, M. A., et al. (2010). Pleiotropic regulatory locus 1 (PRL1) integrates the regulation of sugar responses with isoprenoid metabolism in Arabidopsis. Mol. Plant 3, 101-112. doi: 10.1093/mp/ssp100
    • (2010) Mol. Plant , vol.3 , pp. 101-112
    • Flores-Perez, U.1    Perez-Gil, J.2    Closa, M.3    Wright, L.P.4    Botella-Pavia, P.5    Phillips, M.A.6
  • 42
    • 0035986769 scopus 로고    scopus 로고
    • A novel higher plant protein tyrosine phosphatase interacts with SNF1-related protein kinases via a KIS (kinase interaction sequence) domain
    • doi: 10.1046/j.1365-313X.2002.01250.x
    • Fordham-Skelton, A. P., Chilley, P., Lumbreras, V., Reignoux, S., Fenton, T. R., Dahm, C. C., et al. (2002). A novel higher plant protein tyrosine phosphatase interacts with SNF1-related protein kinases via a KIS (kinase interaction sequence) domain. Plant J. 29, 705-715. doi: 10.1046/j.1365-313X.2002.01250.x
    • (2002) Plant J. , vol.29 , pp. 705-715
    • Fordham-Skelton, A.P.1    Chilley, P.2    Lumbreras, V.3    Reignoux, S.4    Fenton, T.R.5    Dahm, C.C.6
  • 43
    • 65249097143 scopus 로고    scopus 로고
    • SnRK1 isoforms AKIN10 and AKIN11 are differentially regulated in Arabidopsis plants under phosphate starvation
    • doi: 10.1104/pp.108.133298
    • Fragoso, S., Espindola, L., Paez-Valencia, J., Gamboa, A., Camacho, Y., Martinez-Barajas, E., et al. (2009). SnRK1 isoforms AKIN10 and AKIN11 are differentially regulated in Arabidopsis plants under phosphate starvation. Plant Physiol. 149, 1906-1916. doi: 10.1104/pp.108.133298
    • (2009) Plant Physiol. , vol.149 , pp. 1906-1916
    • Fragoso, S.1    Espindola, L.2    Paez-Valencia, J.3    Gamboa, A.4    Camacho, Y.5    Martinez-Barajas, E.6
  • 44
    • 0037067666 scopus 로고    scopus 로고
    • The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • doi: 10.1074/jbc.M202489200
    • Fryer, L. G., Parbu-Patel, A., and Carling, D. (2002). The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways. J. Biol. Chem. 277, 25226-25232. doi: 10.1074/jbc.M202489200
    • (2002) J. Biol. Chem. , vol.277 , pp. 25226-25232
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 45
    • 84866354633 scopus 로고    scopus 로고
    • Role of AGC kinases in plant growth and stress responses
    • doi: 10.1007/s00018-012-1093-3
    • Garcia, A. V., Al-Yousif, M., and Hirt, H. (2012). Role of AGC kinases in plant growth and stress responses. Cell. Mol. Life Sci. 69, 3259-3267. doi: 10.1007/s00018-012-1093-3
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 3259-3267
    • Garcia, A.V.1    Al-Yousif, M.2    Hirt, H.3
  • 46
    • 79952114408 scopus 로고    scopus 로고
    • The PP1-R6 protein phosphatase holoenzyme is involved in the glucose-induced dephosphorylation and inactivation of AMP-activated protein kinase, a key regulator of insulin secretion, in MIN6 beta cells
    • doi: 10.1096/fj.10-166306
    • Garcia-Haro, L., Garcia-Gimeno, M. A., Neumann, D., Beullens, M., Bollen, M., and Sanz, P. (2010). The PP1-R6 protein phosphatase holoenzyme is involved in the glucose-induced dephosphorylation and inactivation of AMP-activated protein kinase, a key regulator of insulin secretion, in MIN6 beta cells. FASEB J. 24, 5080-5091. doi: 10.1096/fj.10-166306
    • (2010) FASEB J. , vol.24 , pp. 5080-5091
    • Garcia-Haro, L.1    Garcia-Gimeno, M.A.2    Neumann, D.3    Beullens, M.4    Bollen, M.5    Sanz, P.6
  • 47
    • 78650731892 scopus 로고    scopus 로고
    • Adenyl cyclases and cAMP in plant signaling-past and present
    • doi: 10.1186/1478-811X-8-15
    • Gehring, C. (2010). Adenyl cyclases and cAMP in plant signaling-past and present. Cell Commun. Signal. 8, 15. doi: 10.1186/1478-811X-8-15
    • (2010) Cell Commun. Signal. , vol.8 , pp. 15
    • Gehring, C.1
  • 48
    • 17844405600 scopus 로고    scopus 로고
    • AKINbeta3, a plant specific SnRK1 protein, is lacking domains present in yeast and mammals non-catalytic beta-subunits
    • doi: 10.1007/s11103-004-5111-1
    • Gissot, L., Polge, C., Bouly, J. P., Lemaitre, T., Kreis, M., and Thomas, M. (2004). AKINbeta3, a plant specific SnRK1 protein, is lacking domains present in yeast and mammals non-catalytic beta-subunits. Plant Mol. Biol. 56, 747-759. doi: 10.1007/s11103-004-5111-1
    • (2004) Plant Mol. Biol. , vol.56 , pp. 747-759
    • Gissot, L.1    Polge, C.2    Bouly, J.P.3    Lemaitre, T.4    Kreis, M.5    Thomas, M.6
  • 49
    • 34249850161 scopus 로고    scopus 로고
    • The role of AMPK and mTOR in nutrient sensing in pancreatic beta-cells
    • doi: 10.1074/jbc.M610631200
    • Gleason, C. E., Lu, D. H., Witters, L. A., Newgard, C. B., and Birnbaum, M. J. (2007). The role of AMPK and mTOR in nutrient sensing in pancreatic beta-cells. J. Biol. Chem. 282, 10341-10351. doi: 10.1074/jbc.M610631200
    • (2007) J. Biol. Chem. , vol.282 , pp. 10341-10351
    • Gleason, C.E.1    Lu, D.H.2    Witters, L.A.3    Newgard, C.B.4    Birnbaum, M.J.5
  • 50
    • 84885168009 scopus 로고    scopus 로고
    • AMP is a true physiological regulator of AMP-activated protein kinase by both allosteric activation and enhancing net phosphorylation
    • doi: 10.1016/j.cmet.2013.08.019
    • Gowans, G. J., Hawley, S. A., Ross, F. A., and Hardie, D. G. (2013). AMP is a true physiological regulator of AMP-activated protein kinase by both allosteric activation and enhancing net phosphorylation. Cell Metab. 18, 556-566. doi: 10.1016/j.cmet.2013.08.019
    • (2013) Cell Metab. , vol.18 , pp. 556-566
    • Gowans, G.J.1    Hawley, S.A.2    Ross, F.A.3    Hardie, D.G.4
  • 51
    • 84880819318 scopus 로고    scopus 로고
    • Phosphorylation of p27(KIP) (1) homologs KRP6 and 7 by SNF1-related protein kinase-1 links plant energy homeostasis and cell proliferation
    • doi: 10.1111/tpj.12218
    • Guerinier, T., Millan, L., Crozet, P., Oury, C., Rey, F., Valot, B., et al. (2013). Phosphorylation of p27(KIP) (1) homologs KRP6 and 7 by SNF1-related protein kinase-1 links plant energy homeostasis and cell proliferation. Plant J. 75, 515-525. doi: 10.1111/tpj.12218
    • (2013) Plant J. , vol.75 , pp. 515-525
    • Guerinier, T.1    Millan, L.2    Crozet, P.3    Oury, C.4    Rey, F.5    Valot, B.6
  • 52
    • 0032127148 scopus 로고    scopus 로고
    • SNF1-related protein kinases: Global regulators of carbon metabolism in plants?
    • doi: 10.1023/A:1006024231305
    • Halford, N. G., and Hardie, D. G. (1998). SNF1-related protein kinases: global regulators of carbon metabolism in plants? Plant Mol. Biol. 37, 735-748. doi: 10.1023/A:1006024231305
    • (1998) Plant Mol. Biol. , vol.37 , pp. 735-748
    • Halford, N.G.1    Hardie, D.G.2
  • 53
    • 0037239022 scopus 로고    scopus 로고
    • Metabolic signalling and carbon partitioning: Role of Snf1-related (SnRK1) protein kinase
    • doi: 10.1093/jxb/erg038
    • Halford, N. G., Hey, S., Jhurreea, D., Laurie, S., Mckibbin, R. S., Paul, M., et al. (2003). Metabolic signalling and carbon partitioning: role of Snf1-related (SnRK1) protein kinase. J. Exp. Bot. 54, 467-475. doi: 10.1093/jxb/erg038
    • (2003) J. Exp. Bot. , vol.54 , pp. 467-475
    • Halford, N.G.1    Hey, S.2    Jhurreea, D.3    Laurie, S.4    Mckibbin, R.S.5    Paul, M.6
  • 54
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K., and Hunter, T. (1995). Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 55
    • 0037392696 scopus 로고    scopus 로고
    • Geminivirus AL2 and L2 proteins interact with and inactivate SNF1 kinase
    • doi: 10.1105/tpc.009530
    • Hao, L., Wang, H., Sunter, G., and Bisaro, D. M. (2003). Geminivirus AL2 and L2 proteins interact with and inactivate SNF1 kinase. Plant Cell 15, 1034-1048. doi: 10.1105/tpc.009530
    • (2003) Plant Cell , vol.15 , pp. 1034-1048
    • Hao, L.1    Wang, H.2    Sunter, G.3    Bisaro, D.M.4
  • 56
    • 34648828532 scopus 로고    scopus 로고
    • AMP-activated/SNF1 protein kinases: Conserved guardians of cellular energy
    • doi: 10.1038/nrm2249
    • Hardie, D. G. (2007). AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy. Nat. Rev. Mol. Cell Biol. 8, 774-785. doi: 10.1038/nrm2249
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 774-785
    • Hardie, D.G.1
  • 57
    • 79952803896 scopus 로고    scopus 로고
    • Hot stuff: Thyroid hormones and AMPK
    • doi: 10.1038/cr.2010.153
    • Hardie, D. G. (2010). Hot stuff: thyroid hormones and AMPK. Cell Res. 20, 1282-1284. doi: 10.1038/cr.2010.153
    • (2010) Cell Res. , vol.20 , pp. 1282-1284
    • Hardie, D.G.1
  • 58
    • 80053035284 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An energy sensor that regulates all aspects of cell function
    • doi: 10.1101/gad.17420111
    • Hardie, D. G. (2011). AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. Genes Dev. 25, 1895-1908. doi: 10.1101/gad.17420111
    • (2011) Genes Dev. , vol.25 , pp. 1895-1908
    • Hardie, D.G.1
  • 59
    • 84868005485 scopus 로고    scopus 로고
    • AMP-activated protein kinase: A target for drugs both ancient and modern
    • doi: 10.1016/j.chembiol.2012.08.019
    • Hardie, D. G., Ross, F. A., and Hawley, S. A. (2012a). AMP-activated protein kinase: a target for drugs both ancient and modern. Chem. Biol. 19, 1222-1236. doi: 10.1016/j.chembiol.2012.08.019
    • (2012) Chem. Biol. , vol.19 , pp. 1222-1236
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 60
    • 84858782079 scopus 로고    scopus 로고
    • AMPK: A nutrient and energy sensor that maintains energy homeostasis
    • doi: 10.1038/nrm3311
    • Hardie, D. G., Ross, F. A., and Hawley, S. A. (2012b). AMPK: a nutrient and energy sensor that maintains energy homeostasis. Nat. Rev. Mol. Cell Biol. 13, 251-262. doi: 10.1038/nrm3311
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 251-262
    • Hardie, D.G.1    Ross, F.A.2    Hawley, S.A.3
  • 61
    • 33745644058 scopus 로고    scopus 로고
    • Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate synthase 5 in response to 2-deoxyglucose
    • doi: 10.1111/j.1365-313X.2006.02780.x
    • Harthill, J. E., Meek, S. E., Morrice, N., Peggie, M. W., Borch, J., Wong, B. H., et al. (2006). Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate synthase 5 in response to 2-deoxyglucose. Plant J. 47, 211-223. doi: 10.1111/j.1365-313X.2006.02780.x
    • (2006) Plant J. , vol.47 , pp. 211-223
    • Harthill, J.E.1    Meek, S.E.2    Morrice, N.3    Peggie, M.W.4    Borch, J.5    Wong, B.H.6
  • 62
    • 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
    • doi: 10.1186/1475-4924-2-28
    • Hawley, S. A., Boudeau, J., Reid, J. L., Mustard, K. J., Udd, L., Makela, T. P., et al. (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. doi: 10.1186/1475-4924-2-28
    • (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    Makela, T.P.6
  • 63
    • 84861222690 scopus 로고    scopus 로고
    • The ancient drug salicylate directly activates AMP-activated protein kinase
    • doi: 10.1126/science.1215327
    • Hawley, S. A., Fullerton, M. D., Ross, F. A., Schertzer, J. D., Chevtzoff, C., Walker, K. J., et al. (2012). The ancient drug salicylate directly activates AMP-activated protein kinase. Science 336, 918-922. doi: 10.1126/science.1215327
    • (2012) Science , vol.336 , pp. 918-922
    • Hawley, S.A.1    Fullerton, M.D.2    Ross, F.A.3    Schertzer, J.D.4    Chevtzoff, C.5    Walker, K.J.6
  • 64
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase
    • doi: 10.1016/j.cmet.2005.05.009
    • Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., et al. (2005). Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Cell Metab. 2, 9-19. doi: 10.1016/j.cmet.2005.05.009
    • (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
  • 65
    • 77956410464 scopus 로고    scopus 로고
    • Use of cells expressing gamma subunit variants to identify diverse mechanisms of AMPK activation
    • doi: 10.1016/j.cmet.2010.04.001
    • Hawley, S. A., Ross, F. A., Chevtzoff, C., Green, K. A., Evans, A., Fogarty, S., et al. (2010). Use of cells expressing gamma subunit variants to identify diverse mechanisms of AMPK activation. Cell Metab. 11, 554-565. doi: 10.1016/j.cmet.2010.04.001
    • (2010) Cell Metab. , vol.11 , pp. 554-565
    • Hawley, S.A.1    Ross, F.A.2    Chevtzoff, C.3    Green, K.A.4    Evans, A.5    Fogarty, S.6
  • 66
    • 0028845251 scopus 로고
    • 2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
    • doi: 10.1074/jbc.270.45.27186
    • 2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J. Biol. Chem. 270, 27186-27191. doi: 10.1074/jbc.270.45.27186
    • (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
  • 67
    • 33845640101 scopus 로고    scopus 로고
    • Regulation of the nucleocytoplasmic distribution of Snf1-Gal83 protein kinase
    • doi: 10.1128/EC.00256-06
    • Hedbacker, K., and Carlson, M. (2006). Regulation of the nucleocytoplasmic distribution of Snf1-Gal83 protein kinase. Eukaryot. Cell 5, 1950-1956. doi: 10.1128/EC.00256-06
    • (2006) Eukaryot. Cell , vol.5 , pp. 1950-1956
    • Hedbacker, K.1    Carlson, M.2
  • 68
    • 38449110592 scopus 로고    scopus 로고
    • SNF1/AMPK pathways in yeast
    • doi: 10.2741/2854
    • Hedbacker, K., and Carlson, M. (2008). SNF1/AMPK pathways in yeast. Front. Biosci. 13:2408-2420. doi: 10.2741/2854
    • (2008) Front. Biosci. , vol.13 , pp. 2408-2420
    • Hedbacker, K.1    Carlson, M.2
  • 69
    • 4444311163 scopus 로고    scopus 로고
    • Pak1 protein kinase regulates activation and nuclear localization of Snf1-Gal83 protein kinase
    • doi: 10.1128/MCB.24.18.8255-8263.2004
    • Hedbacker, K., Hong, S.-P., and Carlson, M. (2004a). Pak1 protein kinase regulates activation and nuclear localization of Snf1-Gal83 protein kinase. Mol. Cell. Biol. 24, 8255-8263. doi: 10.1128/MCB.24.18.8255-8263.2004
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8255-8263
    • Hedbacker, K.1    Hong, S.-P.2    Carlson, M.3
  • 70
    • 1342282918 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase regulates the subcellular localization of Snf1-Sip1 protein kinase
    • doi: 10.1128/MCB.24.5.1836-1843.2004
    • Hedbacker, K., Townley, R., and Carlson, M. (2004b). Cyclic AMP-dependent protein kinase regulates the subcellular localization of Snf1-Sip1 protein kinase. Mol. Cell. Biol. 24, 1836-1843. doi: 10.1128/MCB.24.5.1836-1843.2004
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1836-1843
    • Hedbacker, K.1    Townley, R.2    Carlson, M.3
  • 71
    • 34249860769 scopus 로고    scopus 로고
    • DNA sequences from Arabidopsis, which encode protein kinases and function as upstream regulators of Snf1 in yeast
    • doi: 10.1074/jbc.M611244200
    • Hey, S., Mayerhofer, H., Halford, N. G., and Dickinson, J. R. (2007). DNA sequences from Arabidopsis, which encode protein kinases and function as upstream regulators of Snf1 in yeast. J. Biol. Chem. 282, 10472-10479. doi: 10.1074/jbc.M611244200
    • (2007) J. Biol. Chem. , vol.282 , pp. 10472-10479
    • Hey, S.1    Mayerhofer, H.2    Halford, N.G.3    Dickinson, J.R.4
  • 72
    • 0041305909 scopus 로고    scopus 로고
    • Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases
    • doi: 10.1073/pnas.1533136100
    • Hong, S. P., Leiper, F. C., Woods, A., Carling, D., and Carlson, M. (2003). Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases. Proc. Natl. Acad. Sci. U.S.A. 100, 8839-8843. doi: 10.1073/pnas.1533136100
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 8839-8843
    • Hong, S.P.1    Leiper, F.C.2    Woods, A.3    Carling, D.4    Carlson, M.5
  • 73
    • 33646828975 scopus 로고    scopus 로고
    • Insulin antagonizes ischemia-induced Thr172 phosphorylation of AMP-activated protein kinase alpha-subunits in heart via hierarchical phosphorylation of Ser485/491
    • doi: 10.1074/jbc.M506850200
    • Horman, S., Vertommen, D., Heath, R., Neumann, D., Mouton, V., Woods, A., et al. (2006). Insulin antagonizes ischemia-induced Thr172 phosphorylation of AMP-activated protein kinase alpha-subunits in heart via hierarchical phosphorylation of Ser485/491. J. Biol. Chem. 281, 5335-5340. doi: 10.1074/jbc.M506850200
    • (2006) J. Biol. Chem. , vol.281 , pp. 5335-5340
    • Horman, S.1    Vertommen, D.2    Heath, R.3    Neumann, D.4    Mouton, V.5    Woods, A.6
  • 74
    • 0038377588 scopus 로고    scopus 로고
    • The Arabidopsis CDPK-SnRK superfamily of protein kinases
    • doi: 10.1104/pp.102.011999
    • Hrabak, E. M., Chan, C. W., Gribskov, M., Harper, J. F., Choi, J. H., Halford, N., et al. (2003). The Arabidopsis CDPK-SnRK superfamily of protein kinases. Plant Physiol. 132, 666-680. doi: 10.1104/pp.102.011999
    • (2003) Plant Physiol. , vol.132 , pp. 666-680
    • Hrabak, E.M.1    Chan, C.W.2    Gribskov, M.3    Harper, J.F.4    Choi, J.H.5    Halford, N.6
  • 75
    • 33845972272 scopus 로고    scopus 로고
    • Regulation of AMP-activated protein kinase by multisite phosphorylation in response to agents that elevate cellular cAMP
    • doi: 10.1074/jbc.M606676200
    • Hurley, R. L., Barre, L. K., Wood, S. D., Anderson, K. A., Kemp, B. E., Means, A. R., et al. (2006). Regulation of AMP-activated protein kinase by multisite phosphorylation in response to agents that elevate cellular cAMP. J. Biol. Chem. 281, 36662-36672. doi: 10.1074/jbc.M606676200
    • (2006) J. Biol. Chem. , vol.281 , pp. 36662-36672
    • Hurley, R.L.1    Barre, L.K.2    Wood, S.D.3    Anderson, K.A.4    Kemp, B.E.5    Means, A.R.6
  • 77
    • 70349330577 scopus 로고    scopus 로고
    • The regulation of protein phosphorylation
    • doi: 10.1042/BST0370627
    • Johnson, L. N. (2009). The regulation of protein phosphorylation. Biochem. Soc. Trans. 37, 627-641. doi: 10.1042/BST0370627
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 627-641
    • Johnson, L.N.1
  • 78
    • 67649703979 scopus 로고    scopus 로고
    • SnRK1 (SNF1-related kinase 1) has a central role in sugar and ABA signalling in Arabidopsis thaliana
    • doi: 10.1111/j.1365-313X.2009.03871.x
    • Jossier, M., Bouly, J. P., Meimoun, P., Arjmand, A., Lessard, P., Hawley, S., et al. (2009). SnRK1 (SNF1-related kinase 1) has a central role in sugar and ABA signalling in Arabidopsis thaliana. Plant J. 59, 316-328. doi: 10.1111/j.1365-313X.2009.03871.x
    • (2009) Plant J. , vol.59 , pp. 316-328
    • Jossier, M.1    Bouly, J.P.2    Meimoun, P.3    Arjmand, A.4    Lessard, P.5    Hawley, S.6
  • 79
    • 33645669336 scopus 로고    scopus 로고
    • A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch
    • doi: 10.1111/j.1365-313X.2006.02704.x
    • Kerk, D., Conley, T. R., Rodriguez, F. A., Tran, H. T., Nimick, M., Muench, D. G., et al. (2006). A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch. Plant J. 46, 400-413. doi: 10.1111/j.1365-313X.2006.02704.x
    • (2006) Plant J. , vol.46 , pp. 400-413
    • Kerk, D.1    Conley, T.R.2    Rodriguez, F.A.3    Tran, H.T.4    Nimick, M.5    Muench, D.G.6
  • 80
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • doi: 10.1038/ncb2152
    • Kim, J., Kundu, M., Viollet, B., and Guan, K. L. (2011). AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 13, 132-141. doi: 10.1038/ncb2152
    • (2011) Nat. Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 81
    • 18944401511 scopus 로고    scopus 로고
    • Role of Tos3, a Snf1 protein kinase kinase, during growth ofSaccharomyces cerevisiae on nonfermentable carbon sources
    • doi: 10.1128/EC.4.5.861-866.2005
    • Kim, M. D., Hong, S. P., and Carlson, M. (2005). Role of Tos3, a Snf1 protein kinase kinase, during growth ofSaccharomyces cerevisiae on nonfermentable carbon sources. Eukaryot. Cell 4, 861-866. doi: 10.1128/EC.4.5.861-866.2005
    • (2005) Eukaryot. Cell , vol.4 , pp. 861-866
    • Kim, M.D.1    Hong, S.P.2    Carlson, M.3
  • 82
    • 0033901074 scopus 로고    scopus 로고
    • Functional identification of anArabidopsis snf4 ortholog by screening for heterologous multicopy suppressors of snf4 deficiency in yeast
    • doi: 10.1046/j.1365-313x.2000.00809.x
    • Kleinow, T., Bhalerao, R., Breuer, F., Umeda, M., Salchert, K., and Koncz, C. (2000). Functional identification of anArabidopsis snf4 ortholog by screening for heterologous multicopy suppressors of snf4 deficiency in yeast. Plant J.23, 115-122. doi: 10.1046/j.1365-313x.2000.00809.x
    • (2000) Plant J. , vol.23 , pp. 115-122
    • Kleinow, T.1    Bhalerao, R.2    Breuer, F.3    Umeda, M.4    Salchert, K.5    Koncz, C.6
  • 83
    • 23344440061 scopus 로고    scopus 로고
    • Trehalose 6-phosphate regulates starch synthesis via posttranslational redox activation of ADP-glucose pyrophosphorylase
    • doi: 10.1073/pnas.0503410102
    • Kolbe, A., Tiessen, A., Schluepmann, H., Paul, M., Ulrich, S., and Geigenberger, P. (2005). Trehalose 6-phosphate regulates starch synthesis via posttranslational redox activation of ADP-glucose pyrophosphorylase. Proc. Natl. Acad. Sci. U.S.A. 102, 11118-11123. doi: 10.1073/pnas.0503410102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 11118-11123
    • Kolbe, A.1    Tiessen, A.2    Schluepmann, H.3    Paul, M.4    Ulrich, S.5    Geigenberger, P.6
  • 84
    • 0036670286 scopus 로고    scopus 로고
    • A geminivirus replication protein interacts with a protein kinase and a motor protein that display different expression patterns during plant development and infection
    • doi: 10.1105/tpc.003681
    • Kong, L. J., and Hanley-Bowdoin, L. (2002). A geminivirus replication protein interacts with a protein kinase and a motor protein that display different expression patterns during plant development and infection. Plant Cell 14, 1817-1832. doi: 10.1105/tpc.003681
    • (2002) Plant Cell , vol.14 , pp. 1817-1832
    • Kong, L.J.1    Hanley-Bowdoin, L.2
  • 85
    • 62549132079 scopus 로고    scopus 로고
    • STARCH-EXCESS4 is a laforin-like phosphoglucan phosphatase required for starch degradation in Arabidopsis thaliana
    • doi: 10.1105/tpc.108.064360
    • Kotting, O., Santelia, D., Edner, C., Eicke, S., Marthaler, T., Gentry, M. S., et al. (2009). STARCH-EXCESS4 is a laforin-like phosphoglucan phosphatase required for starch degradation in Arabidopsis thaliana. Plant Cell 21, 334-346. doi: 10.1105/tpc.108.064360
    • (2009) Plant Cell , vol.21 , pp. 334-346
    • Kotting, O.1    Santelia, D.2    Edner, C.3    Eicke, S.4    Marthaler, T.5    Gentry, M.S.6
  • 86
    • 43549110569 scopus 로고    scopus 로고
    • Characterization ofArabidopsis and rice DWD proteins and their roles as substrate receptors for CUL4-RING E3 ubiquitin ligases
    • doi: 10.1105/tpc.107.055418
    • Lee, J. H., Terzaghi, W., Gusmaroli, G., Charron, J. B., Yoon, H. J., Chen, H., et al. (2008). Characterization ofArabidopsis and rice DWD proteins and their roles as substrate receptors for CUL4-RING E3 ubiquitin ligases. Plant Cell 20, 152-167. doi: 10.1105/tpc.107.055418
    • (2008) Plant Cell , vol.20 , pp. 152-167
    • Lee, J.H.1    Terzaghi, W.2    Gusmaroli, G.3    Charron, J.B.4    Yoon, H.J.5    Chen, H.6
  • 87
    • 77449150559 scopus 로고    scopus 로고
    • Coordinated responses to oxygen and sugar deficiency allow rice seedlings to tolerate flooding
    • doi: 10.1126/scisignal.2000333
    • Lee, K. W., Chen, P. W., Lu, C. A., Chen, S., Ho, T. H., and Yu, S. M. (2009). Coordinated responses to oxygen and sugar deficiency allow rice seedlings to tolerate flooding. Sci. Signal. 2, ra61. doi: 10.1126/scisignal.2000333
    • (2009) Sci. Signal. , vol.2
    • Lee, K.W.1    Chen, P.W.2    Lu, C.A.3    Chen, S.4    Ho, T.H.5    Yu, S.M.6
  • 88
    • 84888203586 scopus 로고    scopus 로고
    • Novel small-molecule AMPK activator orally exerts beneficial effects on diabetic db/db mice
    • doi: 10.1016/j.taap.2013.09.006
    • Li, Y. Y., Yu, L. F., Zhang, L. N., Qiu, B. Y., Su, M. B., Wu, F., et al. (2013). Novel small-molecule AMPK activator orally exerts beneficial effects on diabetic db/db mice. Toxicol. Appl. Pharmacol. 273, 325-334. doi: 10.1016/j.taap.2013.09.006
    • (2013) Toxicol. Appl. Pharmacol. , vol.273 , pp. 325-334
    • Li, Y.Y.1    Yu, L.F.2    Zhang, L.N.3    Qiu, B.Y.4    Su, M.B.5    Wu, F.6
  • 89
    • 75749104187 scopus 로고    scopus 로고
    • AMPK as a mediator of hormonal signalling
    • doi: 10.1677/JME-09-0063
    • Lim, C. T., Kola, B., and Korbonits, M. (2010). AMPK as a mediator of hormonal signalling. J. Mol. Endocrinol. 44, 87-97. doi: 10.1677/JME-09-0063
    • (2010) J. Mol. Endocrinol. , vol.44 , pp. 87-97
    • Lim, C.T.1    Kola, B.2    Korbonits, M.3
  • 90
    • 70349096755 scopus 로고    scopus 로고
    • Uncoupling of oxidative phosphorylation by curcumin: Implication of its cellular mechanism of action
    • doi: 10.1016/j.bbrc.2009.08.121
    • Lim, H. W., Lim, H. Y., and Wong, K. P. (2009). Uncoupling of oxidative phosphorylation by curcumin: implication of its cellular mechanism of action. Biochem. Biophys. Res. Commun. 389, 187-192. doi: 10.1016/j.bbrc.2009.08.121
    • (2009) Biochem. Biophys. Res. Commun. , vol.389 , pp. 187-192
    • Lim, H.W.1    Lim, H.Y.2    Wong, K.P.3
  • 91
    • 84897035269 scopus 로고    scopus 로고
    • SnRK1A-interacting negative regulators modulate the nutrient starvation signaling sensor SnRK1 in source-sink communication in cereal seedlings under abiotic stress
    • doi: 10.1105/tpc.113.121939
    • Lin, C. R., Lee, K. W., Chen, C. Y., Hong, Y. F., Chen, J. L., Lu, C. A., et al. (2014). SnRK1A-interacting negative regulators modulate the nutrient starvation signaling sensor SnRK1 in source-sink communication in cereal seedlings under abiotic stress. Plant Cell 26, 808-827. doi: 10.1105/tpc.113.121939
    • (2014) Plant Cell , vol.26 , pp. 808-827
    • Lin, C.R.1    Lee, K.W.2    Chen, C.Y.3    Hong, Y.F.4    Chen, J.L.5    Lu, C.A.6
  • 92
    • 0038644946 scopus 로고    scopus 로고
    • Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing
    • doi: 10.1074/jbc.M212818200
    • Lin, S. S., Manchester, J. K., and Gordon, J. I. (2003). Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J. Biol. Chem. 278, 13390-13397. doi: 10.1074/jbc.M212818200
    • (2003) J. Biol. Chem. , vol.278 , pp. 13390-13397
    • Lin, S.S.1    Manchester, J.K.2    Gordon, J.I.3
  • 93
    • 84863012559 scopus 로고    scopus 로고
    • Functional dissection of lysine deacetylases reveals that HDAC1 and p300 regulate AMPK
    • doi: 10.1038/nature10804
    • Lin, Y. Y., Kiihl, S., Suhail, Y., Liu, S. Y., Chou, Y. H., Kuang, Z., et al. (2012). Functional dissection of lysine deacetylases reveals that HDAC1 and p300 regulate AMPK. Nature 482, 251-255. doi: 10.1038/nature10804
    • (2012) Nature , vol.482 , pp. 251-255
    • Lin, Y.Y.1    Kiihl, S.2    Suhail, Y.3    Liu, S.Y.4    Chou, Y.H.5    Kuang, Z.6
  • 94
    • 84892981163 scopus 로고    scopus 로고
    • Retraction: Functional dissection of lysine deacetylases reveals that HDAC1 and p300 regulate AMPK
    • doi: 10.1038/nature12727
    • Lin, Y.-Y., Kiihl, S., Suhail, Y., Liu, S.-Y., Chou, Y.-H., Kuang, Z., et al. (2013). Retraction: functional dissection of lysine deacetylases reveals that HDAC1 and p300 regulate AMPK. Nature 503, 146-146. doi: 10.1038/nature12727
    • (2013) Nature , vol.503 , pp. 146
    • Lin, Y.-Y.1    Kiihl, S.2    Suhail, Y.3    Liu, S.-Y.4    Chou, Y.-H.5    Kuang, Z.6
  • 95
    • 62149143727 scopus 로고    scopus 로고
    • Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis
    • doi: 10.1016/j.cell.2009.01.033
    • Lin, Y. Y., Lu, J. Y., Zhang, J., Walter, W., Dang, W., Wan, J., et al. (2009). Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 136, 1073-1084. doi: 10.1016/j.cell.2009.01.033
    • (2009) Cell , vol.136 , pp. 1073-1084
    • Lin, Y.Y.1    Lu, J.Y.2    Zhang, J.3    Walter, W.4    Dang, W.5    Wan, J.6
  • 96
    • 79959963047 scopus 로고    scopus 로고
    • Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop
    • doi: 10.4161/auto.7.7.15451
    • Löffler, A. S., Alers, S., Dieterle, A. M., Keppeler, H., Franz-Wachtel, M., Kundu, M., et al. (2011). Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop. Autophagy 7, 696-706. doi: 10.4161/auto.7.7.15451
    • (2011) Autophagy , vol.7 , pp. 696-706
    • Löffler, A.S.1    Alers, S.2    Dieterle, A.M.3    Keppeler, H.4    Franz-Wachtel, M.5    Kundu, M.6
  • 97
    • 67349227190 scopus 로고    scopus 로고
    • Maize AKINbetagamma dimerizes through the KIS/CBM domain and assembles into SnRK1 complexes
    • doi: 10.1016/j.febslet.2009.05.022
    • Lopez-Paz, C., Vilela, B., Riera, M., Pages, M., and Lumbreras, V. (2009). Maize AKINbetagamma dimerizes through the KIS/CBM domain and assembles into SnRK1 complexes. FEBS Lett. 583, 1887-1894. doi: 10.1016/j.febslet.2009.05.022
    • (2009) FEBS Lett. , vol.583 , pp. 1887-1894
    • Lopez-Paz, C.1    Vilela, B.2    Riera, M.3    Pages, M.4    Lumbreras, V.5
  • 98
    • 0037241192 scopus 로고    scopus 로고
    • Antisense repression of StubGAL83 affects root and tuber development in potato
    • doi: 10.1046/j.1365-313X.2003.016015.x
    • Lovas, A., Bimbo, A., Szabo, L., and Banfalvi, Z. (2003a). Antisense repression of StubGAL83 affects root and tuber development in potato. Plant J. 33, 139-147. doi: 10.1046/j.1365-313X.2003.016015.x
    • (2003) Plant J. , vol.33 , pp. 139-147
    • Lovas, A.1    Bimbo, A.2    Szabo, L.3    Banfalvi, Z.4
  • 99
    • 0242409828 scopus 로고    scopus 로고
    • Functional diversity of potato SNF1-related kinases tested in Saccharomyces cerevisiae
    • doi: 10.1016/j.gene.2003.08.001
    • Lovas, A., Sos-Hegedus, A., Bimbo, A., and Banfalvi, Z. (2003b). Functional diversity of potato SNF1-related kinases tested in Saccharomyces cerevisiae. Gene 321, 123-129. doi: 10.1016/j.gene.2003.08.001
    • (2003) Gene , vol.321 , pp. 123-129
    • Lovas, A.1    Sos-Hegedus, A.2    Bimbo, A.3    Banfalvi, Z.4
  • 100
    • 35348855772 scopus 로고    scopus 로고
    • The SnRK1A protein kinase plays a key role in sugar signaling during germination and seedling growth of rice
    • doi: 10.1105/tpc.105.037887
    • Lu, C. A., Lin, C. C., Lee, K. W., Chen, J. L., Huang, L. F., Ho, S. L., et al. (2007). The SnRK1A protein kinase plays a key role in sugar signaling during germination and seedling growth of rice. Plant Cell 19, 2484-2499. doi: 10.1105/tpc.105.037887
    • (2007) Plant Cell , vol.19 , pp. 2484-2499
    • Lu, C.A.1    Lin, C.C.2    Lee, K.W.3    Chen, J.L.4    Huang, L.F.5    Ho, S.L.6
  • 101
    • 80052939858 scopus 로고    scopus 로고
    • Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction
    • doi: 10.1016/j.cell.2011.07.044
    • Lu, J. Y., Lin, Y. Y., Sheu, J. C., Wu, J. T., Lee, F. J., Chen, Y., et al. (2011). Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction. Cell 146, 969-979. doi: 10.1016/j.cell.2011.07.044
    • (2011) Cell , vol.146 , pp. 969-979
    • Lu, J.Y.1    Lin, Y.Y.2    Sheu, J.C.3    Wu, J.T.4    Lee, F.J.5    Chen, Y.6
  • 102
    • 0035093444 scopus 로고    scopus 로고
    • Domain fusion between SNF1-related kinase subunits during plant evolution
    • doi: 10.1093/embo-reports/kve001
    • Lumbreras, V., Alba, M. M., Kleinow, T., Koncz, C., and Pages, M. (2001). Domain fusion between SNF1-related kinase subunits during plant evolution. EMBO Rep. 2, 55-60. doi: 10.1093/embo-reports/kve001
    • (2001) EMBO Rep. , vol.2 , pp. 55-60
    • Lumbreras, V.1    Alba, M.M.2    Kleinow, T.3    Koncz, C.4    Pages, M.5
  • 103
    • 33745530598 scopus 로고    scopus 로고
    • Sugar-induced increases in trehalose 6-phosphate are correlated with redox activation of ADPglucose pyrophosphorylase and higher rates of starch synthesis in Arabidopsis thaliana
    • doi: 10.1042/BJ20060083
    • Lunn, J. E., Feil, R., Hendriks, J. H., Gibon, Y., Morcuende, R., Osuna, D., et al. (2006). Sugar-induced increases in trehalose 6-phosphate are correlated with redox activation of ADPglucose pyrophosphorylase and higher rates of starch synthesis in Arabidopsis thaliana. Biochem. J. 397, 139-148. doi: 10.1042/BJ20060083
    • (2006) Biochem. J. , vol.397 , pp. 139-148
    • Lunn, J.E.1    Feil, R.2    Hendriks, J.H.3    Gibon, Y.4    Morcuende, R.5    Osuna, D.6
  • 104
    • 79956031909 scopus 로고    scopus 로고
    • Wheat grain development is characterized by remarkable trehalose 6-phosphate accumulation pregrain filling: Tissue distribution and relationship to SNF1-related protein kinase1 activity
    • doi: 10.1104/pp.111.174524
    • Martinez-Barajas, E., Delatte, T., Schluepmann, H., De Jong, G. J., Somsen, G. W., Nunes, C., et al. (2011). Wheat grain development is characterized by remarkable trehalose 6-phosphate accumulation pregrain filling: tissue distribution and relationship to SNF1-related protein kinase1 activity. Plant Physiol. 156, 373-381. doi: 10.1104/pp.111.174524
    • (2011) Plant Physiol. , vol.156 , pp. 373-381
    • Martinez-Barajas, E.1    Delatte, T.2    Schluepmann, H.3    De Jong, G.J.4    Somsen, G.W.5    Nunes, C.6
  • 105
    • 80455160062 scopus 로고    scopus 로고
    • ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-activated protein kinase
    • doi: 10.1016/j.cmet.2011.09.009
    • Mayer, F. V., Heath, R., Underwood, E., Sanders, M. J., Carmena, D., Mccartney, R. R., et al. (2011). ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-activated protein kinase. Cell Metab. 14, 707-714. doi: 10.1016/j.cmet.2011.09.009
    • (2011) Cell Metab. , vol.14 , pp. 707-714
    • Mayer, F.V.1    Heath, R.2    Underwood, E.3    Sanders, M.J.4    Carmena, D.5    Mccartney, R.R.6
  • 106
    • 57849090443 scopus 로고    scopus 로고
    • The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor
    • doi: 10.1016/j.cmet.2008.11.008
    • McBride, A., Ghilagaber, S., Nikolaev, A., and Hardie, D. G. (2009). The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor. Cell Metab. 9, 23-34. doi: 10.1016/j.cmet.2008.11.008
    • (2009) Cell Metab. , vol.9 , pp. 23-34
    • McBride, A.1    Ghilagaber, S.2    Nikolaev, A.3    Hardie, D.G.4
  • 107
    • 21344472380 scopus 로고    scopus 로고
    • Snf1 kinase complexes with different beta subunits display stress-dependent preferences for the three Snf1-activating kinases
    • doi: 10.1007/s00294-005-0576-2
    • McCartney, R. R., Rubenstein, E. M., and Schmidt, M. C. (2005). Snf1 kinase complexes with different beta subunits display stress-dependent preferences for the three Snf1-activating kinases. Curr. Genet. 47, 335-344. doi: 10.1007/s00294-005-0576-2
    • (2005) Curr. Genet. , vol.47 , pp. 335-344
    • McCartney, R.R.1    Rubenstein, E.M.2    Schmidt, M.C.3
  • 108
    • 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
    • doi: 10.1074/jbc.M104418200
    • McCartney, R. R., and Schmidt, M. C. (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. doi: 10.1074/jbc.M104418200
    • (2001) J. Biol. Chem. , vol.276 , pp. 36460-36466
    • McCartney, R.R.1    Schmidt, M.C.2
  • 109
    • 38449083934 scopus 로고    scopus 로고
    • AMPK and transcriptional regulation
    • doi: 10.2741/2907
    • McGee, S. L., and Hargreaves, M. (2008). AMPK and transcriptional regulation. Front. Biosci. 13:3022-3033. doi: 10.2741/2907
    • (2008) Front. Biosci. , vol.13 , pp. 3022-3033
    • McGee, S.L.1    Hargreaves, M.2
  • 110
    • 1842484296 scopus 로고    scopus 로고
    • AMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus
    • doi: 10.1038/nature02440
    • Minokoshi, Y., Alquier, T., Furukawa, N., Kim, Y. B., Lee, A., Xue, B. Z., et al. (2004). AMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus. Nature 428, 569-574. doi: 10.1038/nature02440
    • (2004) Nature , vol.428 , pp. 569-574
    • Minokoshi, Y.1    Alquier, T.2    Furukawa, N.3    Kim, Y.B.4    Lee, A.5    Xue, B.Z.6
  • 111
    • 0030870168 scopus 로고    scopus 로고
    • Posttranslational modifications of the 5′-AMP-activated protein kinase beta1 subunit
    • doi: 10.1074/jbc.272.39.24475
    • Mitchelhill, K. I., Michell, B. J., House, C. M., Stapleton, D., Dyck, J., Gamble, J., et al. (1997). Posttranslational modifications of the 5′-AMP-activated protein kinase beta1 subunit. J. Biol. Chem. 272, 24475-24479. doi: 10.1074/jbc.272.39.24475
    • (1997) J. Biol. Chem. , vol.272 , pp. 24475-24479
    • Mitchelhill, K.I.1    Michell, B.J.2    House, C.M.3    Stapleton, D.4    Dyck, J.5    Gamble, J.6
  • 112
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • doi: 10.1074/jbc.M604399200
    • Momcilovic, M., Hong, S. P., and Carlson, M. (2006). Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro. J. Biol. Chem. 281, 25336-25343. doi: 10.1074/jbc.M604399200
    • (2006) J. Biol. Chem. , vol.281 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 113
    • 77955098709 scopus 로고    scopus 로고
    • The laforin-malin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase beta subunits
    • doi: 10.1091/mbc.E10-03-0227
    • Moreno, D., Towler, M. C., Hardie, D. G., Knecht, E., and Sanz, P. (2010). The laforin-malin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase beta subunits. Mol. Biol. Cell 21, 2578-2588. doi: 10.1091/mbc.E10-03-0227
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2578-2588
    • Moreno, D.1    Towler, M.C.2    Hardie, D.G.3    Knecht, E.4    Sanz, P.5
  • 114
    • 70350347981 scopus 로고    scopus 로고
    • Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
    • doi: 10.1016/j.biocel.2009.07.002
    • Moreno, D., Viana, R., and Sanz, P. (2009). Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase. Int. J. Biochem. Cell Biol. 41, 2431-2439. doi: 10.1016/j.biocel.2009.07.002
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 2431-2439
    • Moreno, D.1    Viana, R.2    Sanz, P.3
  • 115
    • 14644435130 scopus 로고    scopus 로고
    • Glucose sensing through the Hxk2-dependent signalling pathway
    • doi: 10.1042/BST0330265
    • Moreno, F., Ahuatzi, D., Riera, A., Palomino, C. A., and Herrero, P. (2005). Glucose sensing through the Hxk2-dependent signalling pathway. Biochem. Soc. Trans. 33, 265-268. doi: 10.1042/BST0330265
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 265-268
    • Moreno, F.1    Ahuatzi, D.2    Riera, A.3    Palomino, C.A.4    Herrero, P.5
  • 116
    • 0028274294 scopus 로고
    • Characterization of tobacco protein kinase NPK5, a homolog ofSaccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae
    • Muranaka, T., Banno, H., and Machida, Y. (1994). Characterization of tobacco protein kinase NPK5, a homolog ofSaccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae. Mol. Cell. Biol. 14, 2958-2965.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2958-2965
    • Muranaka, T.1    Banno, H.2    McHida, Y.3
  • 117
    • 33644833886 scopus 로고    scopus 로고
    • Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family
    • doi: 10.1016/j.str.2005.12.008
    • Nayak, V., Zhao, K., Wyce, A., Schwartz, M. F., Lo, W. S., Berger, S. L., et al. (2006). Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family. Structure 14, 477-485. doi: 10.1016/j.str.2005.12.008
    • (2006) Structure , vol.14 , pp. 477-485
    • Nayak, V.1    Zhao, K.2    Wyce, A.3    Schwartz, M.F.4    Lo, W.S.5    Berger, S.L.6
  • 118
    • 33744955786 scopus 로고    scopus 로고
    • Similar protein phosphatases control starch metabolism in plants and glycogen metabolism in mammals
    • doi: 10.1074/jbc.M600519200
    • Niittyla, T., Comparot-Moss, S., Lue, W. L., Messerli, G., Trevisan, M., Seymour, M. D., et al. (2006). Similar protein phosphatases control starch metabolism in plants and glycogen metabolism in mammals. J. Biol. Chem. 281, 11815-11818. doi: 10.1074/jbc.M600519200
    • (2006) J. Biol. Chem. , vol.281 , pp. 11815-11818
    • Niittyla, T.1    Comparot-Moss, S.2    Lue, W.L.3    Messerli, G.4    Trevisan, M.5    Seymour, M.D.6
  • 119
    • 84879727015 scopus 로고    scopus 로고
    • The trehalose 6-phosphate/SnRK1 signaling pathway primes growth recovery following relief of sink limitation
    • doi: 10.1104/pp.113.220657
    • Nunes, C., O'Hara, L. E., Primavesi, L. F., Delatte, T. L., Schluepmann, H., Somsen, G. W., et al. (2013a). The trehalose 6-phosphate/SnRK1 signaling pathway primes growth recovery following relief of sink limitation. Plant Physiol. 162, 1720-1732. doi: 10.1104/pp.113.220657
    • (2013) Plant Physiol. , vol.162 , pp. 1720-1732
    • Nunes, C.1    O'Hara, L.E.2    Primavesi, L.F.3    Delatte, T.L.4    Schluepmann, H.5    Somsen, G.W.6
  • 120
    • 84871140527 scopus 로고    scopus 로고
    • Inhibition of SnRK1 by metabolites: Tissue-dependent effects and cooperative inhibition by glucose 1-phosphate in combination with trehalose 6-phosphate
    • doi: 10.1016/j.plaphy.2012.11.011
    • Nunes, C., Primavesi, L. F., Patel, M. K., Martinez-Barajas, E., Powers, S. J., Sagar, R., et al. (2013b). Inhibition of SnRK1 by metabolites: tissue-dependent effects and cooperative inhibition by glucose 1-phosphate in combination with trehalose 6-phosphate. Plant Physiol. Biochem. 63, 89-98. doi: 10.1016/j.plaphy.2012.11.011
    • (2013) Plant Physiol. Biochem. , vol.63 , pp. 89-98
    • Nunes, C.1    Primavesi, L.F.2    Patel, M.K.3    Martinez-Barajas, E.4    Powers, S.J.5    Sagar, R.6
  • 121
    • 78650606464 scopus 로고    scopus 로고
    • beta-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK)
    • doi: 10.1073/pnas.1009705107
    • Oakhill, J. S., Chen, Z. P., Scott, J. W., Steel, R., Castelli, L. A., Ling, N., et al. (2010). beta-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK). Proc. Natl. Acad. Sci. U.S.A. 107, 19237-19241. doi: 10.1073/pnas.1009705107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 122
    • 84857687439 scopus 로고    scopus 로고
    • AMPK functions as an adenylate charge-regulated protein kinase. Trends Endocrinol
    • doi: 10.1016/j.tem.2011.12.006
    • 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. doi: 10.1016/j.tem.2011.12.006
    • (2012) Metab. , vol.23 , pp. 125-132
    • Oakhill, J.S.1    Scott, J.W.2    Kemp, B.E.3
  • 123
    • 79959338922 scopus 로고    scopus 로고
    • AMPK is a direct adenylate charge-regulated protein kinase
    • doi: 10.1126/science.1200094
    • Oakhill, J. S., Steel, R., Chen, Z. P., Scott, J. W., Ling, N., Tam, S., et al. (2011). AMPK is a direct adenylate charge-regulated protein kinase. Science 332, 1433-1435. doi: 10.1126/science.1200094
    • (2011) Science , vol.332 , pp. 1433-1435
    • Oakhill, J.S.1    Steel, R.2    Chen, Z.P.3    Scott, J.W.4    Ling, N.5    Tam, S.6
  • 124
    • 70549086229 scopus 로고    scopus 로고
    • Large-scale proteomics analysis of the human kinome
    • doi: 10.1074/mcp.M800588-MCP200
    • Oppermann, F. S., Gnad, F., Olsen, J. V., Hornberger, R., Greff, Z., Kéri, G., et al. (2009). Large-scale proteomics analysis of the human kinome. Mol. Cell. Proteomics 8, 1751-1764. doi: 10.1074/mcp.M800588-MCP200
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1751-1764
    • Oppermann, F.S.1    Gnad, F.2    Olsen, J.V.3    Hornberger, R.4    Greff, Z.5    Kéri, G.6
  • 125
    • 0034659785 scopus 로고    scopus 로고
    • Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain
    • doi: 10.1042/0264-6021:3480607
    • Owen, M. R., Doran, E., and Halestrap, A. P. (2000). Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain. Biochem. J. 348(Pt 3), 607-614. doi: 10.1042/0264-6021:3480607
    • (2000) Biochem. J. , vol.348 , Issue.PART 3 , pp. 607-614
    • Owen, M.R.1    Doran, E.2    Halestrap, A.P.3
  • 126
    • 33846945033 scopus 로고    scopus 로고
    • Conserved alpha-helix acts as autoinhibitory sequence in AMP-activated protein kinase alpha subunits
    • doi: 10.1074/jbc.M605790200
    • Pang, T., Xiong, B., Li, J. Y., Qiu, B. Y., Jin, G. Z., Shen, J. K., et al. (2007). Conserved alpha-helix acts as autoinhibitory sequence in AMP-activated protein kinase alpha subunits. J. Biol. Chem. 282, 495-506. doi: 10.1074/jbc.M605790200
    • (2007) J. Biol. Chem. , vol.282 , pp. 495-506
    • Pang, T.1    Xiong, B.2    Li, J.Y.3    Qiu, B.Y.4    Jin, G.Z.5    Shen, J.K.6
  • 127
    • 47049103144 scopus 로고    scopus 로고
    • Small molecule antagonizes autoinhibition and activates AMP-activated protein kinase in cells
    • doi: 10.1074/jbc.M710114200
    • Pang, T., Zhang, Z. S., Gu, M., Qiu, B. Y., Yu, L. F., Cao, P. R., et al. (2008). Small molecule antagonizes autoinhibition and activates AMP-activated protein kinase in cells. J. Biol. Chem. 283, 16051-16060. doi: 10.1074/jbc.M710114200
    • (2008) J. Biol. Chem. , vol.283 , pp. 16051-16060
    • Pang, T.1    Zhang, Z.S.2    Gu, M.3    Qiu, B.Y.4    Yu, L.F.5    Cao, P.R.6
  • 128
    • 79960145005 scopus 로고    scopus 로고
    • Nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in wheat endosperm at serine-404 by an SNF1-related protein kinase allosterically inhibited by ribose-5-phosphate
    • doi: 10.1104/pp.111.177261
    • Piattoni, C. V., Bustos, D. M., Guerrero, S. A., and Iglesias, A. A. (2011). Nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in wheat endosperm at serine-404 by an SNF1-related protein kinase allosterically inhibited by ribose-5-phosphate. Plant Physiol. 156, 1337-1350. doi: 10.1104/pp.111.177261
    • (2011) Plant Physiol. , vol.156 , pp. 1337-1350
    • Piattoni, C.V.1    Bustos, D.M.2    Guerrero, S.A.3    Iglesias, A.A.4
  • 129
    • 35748940645 scopus 로고    scopus 로고
    • N-myristoylation regulates the SnRK1 pathway in Arabidopsis
    • doi: 10.1105/tpc.107.051870
    • Pierre, M., Traverso, J. A., Boisson, B., Domenichini, S., Bouchez, D., Giglione, C., et al. (2007). N-myristoylation regulates the SnRK1 pathway in Arabidopsis. Plant Cell 19, 2804-2821. doi: 10.1105/tpc.107.051870
    • (2007) Plant Cell , vol.19 , pp. 2804-2821
    • Pierre, M.1    Traverso, J.A.2    Boisson, B.3    Domenichini, S.4    Bouchez, D.5    Giglione, C.6
  • 130
    • 33846290287 scopus 로고    scopus 로고
    • SNF1/AMPK/SnRK1 kinases, global regulators at the heart of energy control?
    • doi: 10.1016/j.tplants.2006.11.005
    • Polge, C., and Thomas, M. (2007). SNF1/AMPK/SnRK1 kinases, global regulators at the heart of energy control?Trends Plant Sci. 12, 20-28. doi: 10.1016/j.tplants.2006.11.005
    • (2007) Trends Plant Sci. , vol.12 , pp. 20-28
    • Polge, C.1    Thomas, M.2
  • 131
    • 0031861675 scopus 로고    scopus 로고
    • Antisense expression of sucrose non-fermenting-1-related protein kinase sequence in potato results in decreased expression of sucrose synthase in tubers and loss of sucrose-inducibility of sucrose synthase transcripts in leaves
    • doi: 10.1046/j.1365-313X.1998.00108.x
    • Purcell, P., Smith, A. M., and Halford, N. G. (1998). Antisense expression of sucrose non-fermenting-1-related protein kinase sequence in potato results in decreased expression of sucrose synthase in tubers and loss of sucrose-inducibility of sucrose synthase transcripts in leaves. Plant J. 14, 195-203. doi: 10.1046/j.1365-313X.1998.00108.x
    • (1998) Plant J. , vol.14 , pp. 195-203
    • Purcell, P.1    Smith, A.M.2    Halford, N.G.3
  • 132
    • 44649099112 scopus 로고    scopus 로고
    • Downregulation of AMP-activated protein kinase by Cidea-mediated ubiquitination and degradation in brown adipose tissue
    • doi: 10.1038/emboj.2008.92
    • Qi, J., Gong, J., Zhao, T., Zhao, J., Lam, P., Ye, J., et al. (2008). Downregulation of AMP-activated protein kinase by Cidea-mediated ubiquitination and degradation in brown adipose tissue. EMBO J. 27, 1537-1548. doi: 10.1038/emboj.2008.92
    • (2008) EMBO J. , vol.27 , pp. 1537-1548
    • Qi, J.1    Gong, J.2    Zhao, T.3    Zhao, J.4    Lam, P.5    Ye, J.6
  • 133
    • 73849134584 scopus 로고    scopus 로고
    • Sucrose non-fermenting kinase 1 (SnRK1) coordinates metabolic and hormonal signals during pea cotyledon growth and differentiation
    • doi: 10.1111/j.1365-313X.2009.04057.x
    • Radchuk, R., Emery, R. J., Weier, D., Vigeolas, H., Geigenberger, P., Lunn, J. E., et al. (2010). Sucrose non-fermenting kinase 1 (SnRK1) coordinates metabolic and hormonal signals during pea cotyledon growth and differentiation. Plant J. 61, 324-338. doi: 10.1111/j.1365-313X.2009.04057.x
    • (2010) Plant J. , vol.61 , pp. 324-338
    • Radchuk, R.1    Emery, R.J.2    Weier, D.3    Vigeolas, H.4    Geigenberger, P.5    Lunn, J.E.6
  • 134
    • 33344466304 scopus 로고    scopus 로고
    • Repressing the expression of the SUCROSE NONFERMENTING-1-RELATED PROTEIN KINASE gene in pea embryo causes pleiotropic defects of maturation similar to an abscisic acid-insensitive phenotype
    • doi: 10.1104/pp.105.071167
    • Radchuk, R., Radchuk, V., Weschke, W., Borisjuk, L., and Weber, H. (2006). Repressing the expression of the SUCROSE NONFERMENTING-1-RELATED PROTEIN KINASE gene in pea embryo causes pleiotropic defects of maturation similar to an abscisic acid-insensitive phenotype. Plant Physiol. 140, 263-278. doi: 10.1104/pp.105.071167
    • (2006) Plant Physiol. , vol.140 , pp. 263-278
    • Radchuk, R.1    Radchuk, V.2    Weschke, W.3    Borisjuk, L.4    Weber, H.5
  • 135
    • 84879224630 scopus 로고    scopus 로고
    • The hybrid four-CBS-domain KINbetagamma-subunit functions as the canonical gamma~subunit of the plant energy sensor SnRK1
    • doi: 10.1111/tpj.12192
    • Ramon, M., Ruelens, P., Li, Y., Sheen, J., Geuten, K., and Rolland, F. (2013). The hybrid four-CBS-domain KINbetagamma-subunit functions as the canonical gamma~subunit of the plant energy sensor SnRK1. Plant J. 75, 11-25. doi: 10.1111/tpj.12192
    • (2013) Plant J. , vol.75 , pp. 11-25
    • Ramon, M.1    Ruelens, P.2    Li, Y.3    Sheen, J.4    Geuten, K.5    Rolland, F.6
  • 136
    • 33646142778 scopus 로고    scopus 로고
    • Glucose-induced repression of PPAR alpha gene expression in pancreatic beta-cells involves PP2A activation and AMPK inactivation
    • doi: 10.1677/jme.1.01965
    • Ravnskjaer, K., Boergesen, M., Dalgaard, L. T., and Mandrup, S. (2006). Glucose-induced repression of PPAR alpha gene expression in pancreatic beta-cells involves PP2A activation and AMPK inactivation. J. Mol. Endocrinol. 36, 289-299. doi: 10.1677/jme.1.01965
    • (2006) J. Mol. Endocrinol. , vol.36 , pp. 289-299
    • Ravnskjaer, K.1    Boergesen, M.2    Dalgaard, L.T.3    Mandrup, S.4
  • 137
    • 15644384598 scopus 로고    scopus 로고
    • AMP-activated protein kinase mediates phenobarbital induction of CYP2B gene expression in hepatocytes and a newly derived human hepatoma cell line
    • doi: 10.1074/jbc.M412711200
    • Rencurel, F., Stenhouse, A., Hawley, S. A., Friedberg, T., Hardie, D. G., Sutherland, C., et al. (2005). AMP-activated protein kinase mediates phenobarbital induction of CYP2B gene expression in hepatocytes and a newly derived human hepatoma cell line. J. Biol. Chem. 280, 4367-4373. doi: 10.1074/jbc.M412711200
    • (2005) J. Biol. Chem. , vol.280 , pp. 4367-4373
    • Rencurel, F.1    Stenhouse, A.2    Hawley, S.A.3    Friedberg, T.4    Hardie, D.G.5    Sutherland, C.6
  • 138
    • 49649115970 scopus 로고    scopus 로고
    • Structural properties of AMP-activated protein kinase: Dimerization, molecular shape, and changes upon ligand binding
    • doi: 10.1074/jbc.M708379200
    • Riek, U., Scholz, R., Konarev, P., Rufer, A., Suter, M., Nazabal, A., et al. (2008). Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding. J. Biol. Chem. 283, 18331-18343. doi: 10.1074/jbc.M708379200
    • (2008) J. Biol. Chem. , vol.283 , pp. 18331-18343
    • Riek, U.1    Scholz, R.2    Konarev, P.3    Rufer, A.4    Suter, M.5    Nazabal, A.6
  • 139
    • 84888427451 scopus 로고    scopus 로고
    • ABI1 and PP2CA phosphatases are negative regulators of Snf1-related protein kinase1 signaling in Arabidopsis
    • doi: 10.1105/tpc.113.114066
    • Rodrigues, A., Adamo, M., Crozet, P., Margalha, L., Confraria, A., Martinho, C., et al. (2013). ABI1 and PP2CA phosphatases are negative regulators of Snf1-related protein kinase1 signaling in Arabidopsis. Plant Cell 25, 3871-3884. doi: 10.1105/tpc.113.114066
    • (2013) Plant Cell , vol.25 , pp. 3871-3884
    • Rodrigues, A.1    Adamo, M.2    Crozet, P.3    Margalha, L.4    Confraria, A.5    Martinho, C.6
  • 140
    • 38049174646 scopus 로고    scopus 로고
    • Access denied: Snf1 activation loop phosphorylation is controlled by availability of the phosphorylated threonine 210 to the PP1 phosphatase
    • doi: 10.1074/jbc.M707957200
    • Rubenstein, E. M., Mccartney, R. R., Zhang, C., Shokat, K. M., Shirra, M. K., Arndt, K. 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. doi: 10.1074/jbc.M707957200
    • (2008) J. Biol. Chem. , vol.283 , pp. 222-230
    • Rubenstein, E.M.1    Mccartney, R.R.2    Zhang, C.3    Shokat, K.M.4    Shirra, M.K.5    Arndt, K.M.6
  • 141
    • 84878695660 scopus 로고    scopus 로고
    • Sumoylation of AMPKbeta2 subunit enhances AMP-activated protein kinase activity
    • 1801-1811+S1-S4
    • Rubio, T., Vernia, S., and Sanz, P. (2013). Sumoylation of AMPKbeta2 subunit enhances AMP-activated protein kinase activity. Mol. Biol. Cell 24, 1801-1811, S1-S4.
    • (2013) Mol. Biol. Cell , vol.24
    • Rubio, T.1    Vernia, S.2    Sanz, P.3
  • 142
    • 27144548462 scopus 로고    scopus 로고
    • Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1
    • doi: 10.1016/j.bbrc.2005.09.181
    • Rudolph, M. J., Amodeo, G. A., Bai, Y., and Tong, L. (2005). Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1. Biochem. Biophys. Res. Commun. 337, 1224-1228. doi: 10.1016/j.bbrc.2005.09.181
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1224-1228
    • Rudolph, M.J.1    Amodeo, G.A.2    Bai, Y.3    Tong, L.4
  • 143
    • 33846103020 scopus 로고    scopus 로고
    • Structure of the Bateman2 domain of yeast Snf4: Dimeric association and relevance for AMP binding
    • doi: 10.1016/j.str.2006.11.014
    • Rudolph, M. J., Amodeo, G. A., Iram, S. H., Hong, S. P., Pirino, G., Carlson, M., et al. (2007). Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP binding. Structure 15, 65-74. doi: 10.1016/j.str.2006.11.014
    • (2007) Structure , vol.15 , pp. 65-74
    • Rudolph, M.J.1    Amodeo, G.A.2    Iram, S.H.3    Hong, S.P.4    Pirino, G.5    Carlson, M.6
  • 144
    • 84861899883 scopus 로고    scopus 로고
    • Heterotrimer-independent regulation of activation-loop phosphorylation of Snf1 protein kinase involves two protein phosphatases
    • doi: 10.1073/pnas.1206280109
    • Ruiz, A., Liu, Y., Xu, X., and Carlson, M. (2012). Heterotrimer-independent regulation of activation-loop phosphorylation of Snf1 protein kinase involves two protein phosphatases. Proc. Natl. Acad. Sci. U.S.A. 109, 8652-8657. doi: 10.1073/pnas.1206280109
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 8652-8657
    • Ruiz, A.1    Liu, Y.2    Xu, X.3    Carlson, M.4
  • 145
    • 79955588701 scopus 로고    scopus 로고
    • Roles of two protein phosphatases, Reg1-Glc7 and Sit4, and glycogen synthesis in regulation of SNF1 protein kinase
    • doi: 10.1073/pnas.1102758108
    • Ruiz, A., Xu, X., and Carlson, M. (2011). Roles of two protein phosphatases, Reg1-Glc7 and Sit4, and glycogen synthesis in regulation of SNF1 protein kinase. Proc. Natl. Acad. Sci. U.S.A. 108, 6349-6354. doi: 10.1073/pnas.1102758108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6349-6354
    • Ruiz, A.1    Xu, X.2    Carlson, M.3
  • 146
    • 84886648461 scopus 로고    scopus 로고
    • Ptc1 protein phosphatase 2C contributes to glucose regulation of SNF1/AMP-activated protein kinase (AMPK) in Saccharomyces cerevisiae
    • doi: 10.1074/jbc.M113.503763
    • Ruiz, A., Xu, X., and Carlson, M. (2013). Ptc1 protein phosphatase 2C contributes to glucose regulation of SNF1/AMP-activated protein kinase (AMPK) in Saccharomyces cerevisiae. J. Biol. Chem. 288, 31052-31058. doi: 10.1074/jbc.M113.503763
    • (2013) J. Biol. Chem. , vol.288 , pp. 31052-31058
    • Ruiz, A.1    Xu, X.2    Carlson, M.3
  • 147
    • 17144474893 scopus 로고    scopus 로고
    • Activity of LKB1 and AMPK-related kinases in skeletal muscle: Effects of contraction, phenformin, and AICAR
    • doi: 10.1152/ajpendo.00074.2004
    • Sakamoto, K., Goransson, 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. doi: 10.1152/ajpendo.00074.2004
    • (2004) Am. J. Physiol. Endocrinol. Metab. , vol.287
    • Sakamoto, K.1    Goransson, O.2    Hardie, D.G.3    Alessi, D.R.4
  • 148
    • 34147152841 scopus 로고    scopus 로고
    • Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    • doi: 10.1042/BJ20061520
    • 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. doi: 10.1042/BJ20061520
    • (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
  • 149
    • 84861906117 scopus 로고    scopus 로고
    • Metabolism control over growth: A case for trehalose-6-phosphate in plants
    • doi: 10.1093/jxb/err311
    • Schluepmann, H., Berke, L., and Sanchez-Perez, G. F. (2012). Metabolism control over growth: a case for trehalose-6-phosphate in plants. J. Exp. Bot. 63, 3379-3390. doi: 10.1093/jxb/err311
    • (2012) J. Exp. Bot. , vol.63 , pp. 3379-3390
    • Schluepmann, H.1    Berke, L.2    Sanchez-Perez, G.F.3
  • 150
    • 70350437313 scopus 로고    scopus 로고
    • Homo-oligomerization and activation of AMP-activated protein kinase are mediated by the kinase domain alphaG-helix
    • doi: 10.1074/jbc.M109.047670
    • Scholz, R., Suter, M., Weimann, T., Polge, C., Konarev, P. V., Thali, R. F., et al. (2009). Homo-oligomerization and activation of AMP-activated protein kinase are mediated by the kinase domain alphaG-helix. J. Biol. Chem. 284, 27425-27437. doi: 10.1074/jbc.M109.047670
    • (2009) J. Biol. Chem. , vol.284 , pp. 27425-27437
    • Scholz, R.1    Suter, M.2    Weimann, T.3    Polge, C.4    Konarev, P.V.5    Thali, R.F.6
  • 151
    • 33748041467 scopus 로고    scopus 로고
    • SNF1-related kinases allow plants to tolerate herbivory by allocating carbon to roots
    • doi: 10.1073/pnas.0602316103
    • Schwachtje, J., Minchin, P. E., Jahnke, S., Van Dongen, J. T., Schittko, U., and Baldwin, I. T. (2006). SNF1-related kinases allow plants to tolerate herbivory by allocating carbon to roots. Proc. Natl. Acad. Sci. U.S.A. 103, 12935-12940. doi: 10.1073/pnas.0602316103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 12935-12940
    • Schwachtje, J.1    Minchin, P.E.2    Jahnke, S.3    Van Dongen, J.T.4    Schittko, U.5    Baldwin, I.T.6
  • 152
    • 85047691317 scopus 로고    scopus 로고
    • CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations
    • doi: 10.1172/JCI19874
    • Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., 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. doi: 10.1172/JCI19874
    • (2004) J. Clin. Invest. , vol.113 , pp. 274-284
    • Scott, J.W.1    Hawley, S.A.2    Green, K.A.3    Anis, M.4    Stewart, G.5    Scullion, G.A.6
  • 153
    • 56049112796 scopus 로고    scopus 로고
    • Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes
    • doi: 10.1016/j.chembiol.2008.10.005
    • Scott, J. W., Van Denderen, B. J., Jorgensen, S. B., Honeyman, J. E., Steinberg, G. R., Oakhill, J. S., et al. (2008). Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes. Chem. Biol. 15, 1220-1230. doi: 10.1016/j.chembiol.2008.10.005
    • (2008) Chem. Biol. , vol.15 , pp. 1220-1230
    • Scott, J.W.1    Van Denderen, B.J.2    Jorgensen, S.B.3    Honeyman, J.E.4    Steinberg, G.R.5    Oakhill, J.S.6
  • 154
    • 77952878619 scopus 로고    scopus 로고
    • Skeletal muscles of Uchl3 knockout mice show polyubiquitinated protein accumulation and stress responses
    • doi: 10.1016/j.neuint.2010.03.021
    • Setsuie, R., Suzuki, M., Tsuchiya, Y., and Wada, K. (2010). Skeletal muscles of Uchl3 knockout mice show polyubiquitinated protein accumulation and stress responses. Neurochem. Int. 56, 911-918. doi: 10.1016/j.neuint.2010.03.021
    • (2010) Neurochem. Int. , vol.56 , pp. 911-918
    • Setsuie, R.1    Suzuki, M.2    Tsuchiya, Y.3    Wada, K.4
  • 155
    • 84893432818 scopus 로고    scopus 로고
    • A redox-dependent mechanism for regulation of AMPK activation by thioredoxin1 during energy starvation
    • doi: 10.1016/j.cmet.2013.12.013
    • Shao, D., Oka, S., Liu, T., Zhai, P., Ago, T., Sciarretta, S., et al. (2014). A redox-dependent mechanism for regulation of AMPK activation by thioredoxin1 during energy starvation. Cell Metab. 19, 232-245. doi: 10.1016/j.cmet.2013.12.013
    • (2014) Cell Metab. , vol.19 , pp. 232-245
    • Shao, D.1    Oka, S.2    Liu, T.3    Zhai, P.4    Ago, T.5    Sciarretta, S.6
  • 156
    • 33845619512 scopus 로고    scopus 로고
    • Geminivirus infection up-regulates the expression of two Arabidopsisprotein kinases related to yeast SNF1-and mammalian AMPK-activating kinases
    • doi: 10.1104/pp.106.088476
    • Shen, W., and Hanley-Bowdoin, L. (2006). Geminivirus infection up-regulates the expression of two Arabidopsisprotein kinases related to yeast SNF1-and mammalian AMPK-activating kinases. Plant Physiol. 142, 1642-1655. doi: 10.1104/pp.106.088476
    • (2006) Plant Physiol. , vol.142 , pp. 1642-1655
    • Shen, W.1    Hanley-Bowdoin, L.2
  • 157
    • 66649086822 scopus 로고    scopus 로고
    • Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate SnRK1 by phosphorylating its activation loop
    • doi: 10.1104/pp.108.132787
    • Shen, W., Reyes, M. I., and Hanley-Bowdoin, L. (2009). Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate SnRK1 by phosphorylating its activation loop. Plant Physiol. 150, 996-1005. doi: 10.1104/pp.108.132787
    • (2009) Plant Physiol. , vol.150 , pp. 996-1005
    • Shen, W.1    Reyes, M.I.2    Hanley-Bowdoin, L.3
  • 158
    • 84886409705 scopus 로고    scopus 로고
    • SUMOylation regulates the SNF1 protein kinase
    • doi: 10.1073/pnas.1304839110
    • Simpson-Lavy, K. J., and Johnston, M. (2013). SUMOylation regulates the SNF1 protein kinase. Proc. Natl. Acad. Sci. U.S.A. 110, 17432-17437. doi: 10.1073/pnas.1304839110
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 17432-17437
    • Simpson-Lavy, K.J.1    Johnston, M.2
  • 159
    • 0033501047 scopus 로고    scopus 로고
    • The Elm1 kinase functions in a mitotic signaling network in budding yeast
    • Sreenivasan, A., and Kellogg, D. (1999). The Elm1 kinase functions in a mitotic signaling network in budding yeast. Mol. Cell. Biol. 19, 7983-7994.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7983-7994
    • Sreenivasan, A.1    Kellogg, D.2
  • 160
  • 161
    • 0034141355 scopus 로고    scopus 로고
    • The regulation of AMP-activated protein kinase by phosphorylation
    • doi: 10.1042/0264-6021:3450437
    • 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(Pt 3), 437-443. doi: 10.1042/0264-6021:3450437
    • (2000) Biochem. J. , vol.345 , Issue.PART 3 , pp. 437-443
    • Stein, S.C.1    Woods, A.2    Jones, N.A.3    Davison, M.D.4    Carling, D.5
  • 162
    • 67650914230 scopus 로고    scopus 로고
    • AMPK in health and disease
    • doi: 10.1152/physrev.00011.2008
    • Steinberg, G. R., and Kemp, B. E. (2009). AMPK in health and disease. Physiol. Rev. 89, 1025-1078. doi: 10.1152/physrev.00011.2008
    • (2009) Physiol. Rev. , vol.89 , pp. 1025-1078
    • Steinberg, G.R.1    Kemp, B.E.2
  • 163
    • 33751552452 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling
    • doi: 10.1016/j.cmet.2006.11.005
    • Steinberg, G. R., Michell, B. J., Van Denderen, B. J., Watt, M. J., Carey, A. L., Fam, B. C., et al. (2006). Tumor necrosis factor alpha-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling. Cell Metab. 4, 465-474. doi: 10.1016/j.cmet.2006.11.005
    • (2006) Cell Metab. , vol.4 , pp. 465-474
    • Steinberg, G.R.1    Michell, B.J.2    Van Denderen, B.J.3    Watt, M.J.4    Carey, A.L.5    Fam, B.C.6
  • 164
    • 0033180353 scopus 로고    scopus 로고
    • Regulation of spinach SNF1-related (SnRK1) kinases by protein kinases and phosphatases is associated with phosphorylation of the T loop and is regulated by 5′-AMP
    • doi: 10.1046/j.1365-313X.1999.00532.x
    • Sugden, C., Crawford, R. M., Halford, N. G., and Hardie, D. G. (1999a). Regulation of spinach SNF1-related (SnRK1) kinases by protein kinases and phosphatases is associated with phosphorylation of the T loop and is regulated by 5′-AMP. Plant J. 19, 433-439. doi: 10.1046/j.1365-313X.1999.00532.x
    • (1999) Plant J. , vol.19 , pp. 433-439
    • Sugden, C.1    Crawford, R.M.2    Halford, N.G.3    Hardie, D.G.4
  • 165
    • 0033134243 scopus 로고    scopus 로고
    • Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro
    • doi: 10.1104/pp.120.1.257
    • Sugden, C., Donaghy, P. G., Halford, N. G., and Hardie, D. G. (1999b). Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro. Plant Physiol. 120, 257-274. doi: 10.1104/pp.120.1.257
    • (1999) Plant Physiol. , vol.120 , pp. 257-274
    • Sugden, C.1    Donaghy, P.G.2    Halford, N.G.3    Hardie, D.G.4
  • 166
    • 33845949733 scopus 로고    scopus 로고
    • Dissecting the role of 5′-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase
    • doi: 10.1074/jbc.M606357200
    • Suter, M., Riek, U., Tuerk, R., Schlattner, U., Wallimann, T., and Neumann, D. (2006). Dissecting the role of 5′-AMP for allosteric stimulation, activation, and deactivation of AMP-activated protein kinase. J. Biol. Chem. 281, 32207-32216. doi: 10.1074/jbc.M606357200
    • (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
  • 167
    • 34250182374 scopus 로고    scopus 로고
    • Leptin stimulates fatty acid oxidation and peroxisome proliferator-activated receptor alpha gene expression in mouse C2C12 myoblasts by changing the subcellular localization of the alpha2 form of AMP-activated protein kinase
    • doi: 10.1128/MCB.02222-06
    • Suzuki, A., Okamoto, S., Lee, S., Saito, K., Shiuchi, T., and Minokoshi, Y. (2007). Leptin stimulates fatty acid oxidation and peroxisome proliferator-activated receptor alpha gene expression in mouse C2C12 myoblasts by changing the subcellular localization of the alpha2 form of AMP-activated protein kinase. Mol. Cell. Biol. 27, 4317-4327. doi: 10.1128/MCB.02222-06
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4317-4327
    • Suzuki, A.1    Okamoto, S.2    Lee, S.3    Saito, K.4    Shiuchi, T.5    Minokoshi, Y.6
  • 168
    • 0028985536 scopus 로고
    • Trehalose synthase: Guard to the gate of glycolysis in yeast?
    • doi: 10.1016/S0968-0004(00)88938-0
    • Thevelein, J. M., and Hohmann, S. (1995). Trehalose synthase: guard to the gate of glycolysis in yeast? Trends Biochem. Sci. 20, 3-10. doi: 10.1016/S0968-0004(00)88938-0
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 3-10
    • Thevelein, J.M.1    Hohmann, S.2
  • 169
    • 0042352390 scopus 로고    scopus 로고
    • Evidence that SNF1-related kinase and hexokinase are involved in separate sugar-signalling pathways modulating post-translational redox activation of ADP-glucose pyrophosphorylase in potato tubers
    • doi: 10.1046/j.1365-313X.2003.01823.x
    • Tiessen, A., Prescha, K., Branscheid, A., Palacios, N., Mckibbin, R., Halford, N. G., et al. (2003). Evidence that SNF1-related kinase and hexokinase are involved in separate sugar-signalling pathways modulating post-translational redox activation of ADP-glucose pyrophosphorylase in potato tubers. Plant J. 35, 490-500. doi: 10.1046/j.1365-313X.2003.01823.x
    • (2003) Plant J. , vol.35 , pp. 490-500
    • Tiessen, A.1    Prescha, K.2    Branscheid, A.3    Palacios, N.4    Mckibbin, R.5    Halford, N.G.6
  • 170
    • 0034073253 scopus 로고    scopus 로고
    • Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate
    • doi: 10.1104/pp.123.1.403
    • Toroser, D., Plaut, Z., and Huber, S. C. (2000). Regulation of a plant SNF1-related protein kinase by glucose-6-phosphate. Plant Physiol. 123, 403-411. doi: 10.1104/pp.123.1.403
    • (2000) Plant Physiol. , vol.123 , pp. 403-411
    • Toroser, D.1    Plaut, Z.2    Huber, S.C.3
  • 171
    • 34047161436 scopus 로고    scopus 로고
    • Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase
    • doi: 10.1126/science.1137503
    • Townley, R., and Shapiro, L. (2007). Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase. Science 315, 1726-1729. doi: 10.1126/science.1137503
    • (2007) Science , vol.315 , pp. 1726-1729
    • Townley, R.1    Shapiro, L.2
  • 172
    • 84857648074 scopus 로고    scopus 로고
    • AKIN10 and FUSCA3 interact to control lateral organ development and phase transitions in Arabidopsis
    • doi: 10.1111/j.1365-313X.2011.04832.x
    • Tsai, A. Y., and Gazzarrini, S. (2012). AKIN10 and FUSCA3 interact to control lateral organ development and phase transitions in Arabidopsis. Plant J. 69, 809-821. doi: 10.1111/j.1365-313X.2011.04832.x
    • (2012) Plant J. , vol.69 , pp. 809-821
    • Tsai, A.Y.1    Gazzarrini, S.2
  • 173
    • 84862819569 scopus 로고    scopus 로고
    • A putative myristoylated 2C-type protein phosphatase, PP2C74, interacts with SnRK1 in Arabidopsis
    • doi: 10.1016/j.febslet.2012.02.019
    • Tsugama, D., Liu, S., and Takano, T. (2012). A putative myristoylated 2C-type protein phosphatase, PP2C74, interacts with SnRK1 in Arabidopsis. FEBS Lett. 586, 693-698. doi: 10.1016/j.febslet.2012.02.019
    • (2012) FEBS Lett. , vol.586 , pp. 693-698
    • Tsugama, D.1    Liu, S.2    Takano, T.3
  • 174
    • 48449084609 scopus 로고    scopus 로고
    • Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: A mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action
    • Turner, N., Li, J. Y., Gosby, A., To, S. W., Cheng, Z., Miyoshi, H., et al. (2008). Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: a mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action. Diabetes Metab. Res. Rev. 57, 1414-1418.
    • (2008) Diabetes Metab. Res. Rev. , vol.57 , pp. 1414-1418
    • Turner, N.1    Li, J.Y.2    Gosby, A.3    To, S.W.4    Cheng, Z.5    Miyoshi, H.6
  • 175
    • 78349276098 scopus 로고    scopus 로고
    • Molecular basis of the core regulatory network in ABA responses: Sensing, signaling and transport
    • doi: 10.1093/pcp/pcq156
    • Umezawa, T., Nakashima, K., Miyakawa, T., Kuromori, T., Tanokura, M., Shinozaki, K., et al. (2010). Molecular basis of the core regulatory network in ABA responses: sensing, signaling and transport. Plant Cell Physiol. 51, 1821-1839. doi: 10.1093/pcp/pcq156
    • (2010) Plant Cell Physiol. , vol.51 , pp. 1821-1839
    • Umezawa, T.1    Nakashima, K.2    Miyakawa, T.3    Kuromori, T.4    Tanokura, M.5    Shinozaki, K.6
  • 176
    • 77957763018 scopus 로고    scopus 로고
    • Ppm1E is an in cellulo AMP-activated protein kinase phosphatase
    • doi: 10.1016/j.cellsig.2010.08.010
    • Voss, M., Paterson, J., Kelsall, I. R., Martin-Granados, C., Hastie, C. J., Peggie, M. W., et al. (2011). Ppm1E is an in cellulo AMP-activated protein kinase phosphatase. Cell. Signal. 23, 114-124. doi: 10.1016/j.cellsig.2010.08.010
    • (2011) Cell. Signal. , vol.23 , pp. 114-124
    • Voss, M.1    Paterson, J.2    Kelsall, I.R.3    Martin-Granados, C.4    Hastie, C.J.5    Peggie, M.W.6
  • 177
    • 0035282062 scopus 로고    scopus 로고
    • Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization
    • doi: 10.1042/0264-6021:3540275
    • Warden, S. M., Richardson, C., O'Donnell, J. Jr., Stapleton, D., Kemp, B. E., and Witters, L. A. (2001). Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization. Biochem. J. 354, 275-283. doi: 10.1042/0264-6021:3540275
    • (2001) Biochem. J. , vol.354 , pp. 275-283
    • Warden, S.M.1    Richardson, C.2    O'Donnell Jr., J.3    Stapleton, D.4    Kemp, B.E.5    Witters, L.A.6
  • 178
    • 70350125202 scopus 로고    scopus 로고
    • The CBL-CIPK Ca(2+)-decoding signaling network: Function and perspectives
    • doi: 10.1111/j.1469-8137.2009.02938.x
    • Weinl, S., and Kudla, J. (2009). The CBL-CIPK Ca(2+)-decoding signaling network: function and perspectives. New Phytol. 184, 517-528. doi: 10.1111/j.1469-8137.2009.02938.x
    • (2009) New Phytol. , vol.184 , pp. 517-528
    • Weinl, S.1    Kudla, J.2
  • 179
    • 0345732634 scopus 로고    scopus 로고
    • Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism
    • doi: 10.1128/MCB.24.1.352-361.2004
    • Wiatrowski, H. A., Van Denderen, B. J., Berkey, C. D., Kemp, B. E., Stapleton, D., and Carlson, M. (2004). Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism. Mol. Cell. Biol. 24, 352-361. doi: 10.1128/MCB.24.1.352-361.2004
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 352-361
    • Wiatrowski, H.A.1    Van Denderen, B.J.2    Berkey, C.D.3    Kemp, B.E.4    Stapleton, D.5    Carlson, M.6
  • 181
    • 0030293885 scopus 로고    scopus 로고
    • Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio
    • doi: 10.1016/S0960-9822(96)00747-6
    • Wilson, W. A., Hawley, S. A., and Hardie, D. G. (1996). Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio. Curr. Biol. 6, 1426-1434. doi: 10.1016/S0960-9822(96)00747-6
    • (1996) Curr. Biol. , vol.6 , pp. 1426-1434
    • Wilson, W.A.1    Hawley, S.A.2    Hardie, D.G.3
  • 182
    • 84857952225 scopus 로고    scopus 로고
    • Trehalose 6-phosphate is required for the onset of leaf senescence associated with high carbon availability
    • doi: 10.1104/pp.111.191908
    • Wingler, A., Delatte, T. L., O'Hara, L. E., Primavesi, L. F., Jhurreea, D., Paul, M. J., et al. (2012). Trehalose 6-phosphate is required for the onset of leaf senescence associated with high carbon availability. Plant Physiol. 158, 1241-1251. doi: 10.1104/pp.111.191908
    • (2012) Plant Physiol. , vol.158 , pp. 1241-1251
    • Wingler, A.1    Delatte, T.L.2    O'Hara, L.E.3    Primavesi, L.F.4    Jhurreea, D.5    Paul, M.J.6
  • 183
    • 47649120869 scopus 로고    scopus 로고
    • Metabolic regulation of leaf senescence: Interactions of sugar signalling with biotic and abiotic stress responses
    • doi: 10.1111/j.1438-8677.2008.00086.x
    • Wingler, A., and Roitsch, T. (2008). Metabolic regulation of leaf senescence: interactions of sugar signalling with biotic and abiotic stress responses. Plant Biol. (Stuttg.) 10(Suppl.1), 50-62. doi: 10.1111/j.1438-8677.2008.00086.x
    • (2008) Plant Biol. (Stuttg.) , vol.10 , Issue.SUPPL. 1 , pp. 50-62
    • Wingler, A.1    Roitsch, T.2
  • 184
    • 23044437445 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells
    • doi: 10.1016/j.cmet.2005.06.005
    • 2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells. Cell Metab. 2, 21-33. doi: 10.1016/j.cmet.2005.06.005
    • (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
  • 185
    • 10744230065 scopus 로고    scopus 로고
    • LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
    • doi: 10.1016/j.cub.2003.10.031
    • Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G., Neumann, D., et al. (2003a). LKB1 is the upstream kinase in the AMP-activated protein kinase cascade. Curr. Biol. 13, 2004-2008. doi: 10.1016/j.cub.2003.10.031
    • (2003) Curr. Biol. , vol.13 , pp. 2004-2008
    • Woods, A.1    Johnstone, S.R.2    Dickerson, K.3    Leiper, F.C.4    Fryer, L.G.5    Neumann, D.6
  • 186
    • 0043210478 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis
    • doi: 10.1074/jbc.M303946200
    • Woods, A., Vertommen, D., Neumann, D., Turk, R., Bayliss, J., Schlattner, U., et al. (2003b). Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis. J. Biol. Chem. 278, 28434-28442. doi: 10.1074/jbc.M303946200
    • (2003) J. Biol. Chem. , vol.278 , pp. 28434-28442
    • Woods, A.1    Vertommen, D.2    Neumann, D.3    Turk, R.4    Bayliss, J.5    Schlattner, U.6
  • 187
    • 78649249525 scopus 로고    scopus 로고
    • Physiological basis for enhanced sucrose accumulation in an engineered sugarcane cell line
    • doi: 10.1071/FP10055
    • Wu, L. G., and Birch, R. G. (2010). Physiological basis for enhanced sucrose accumulation in an engineered sugarcane cell line. Funct. Plant Biol. 37, 1161-1174. doi: 10.1071/FP10055
    • (2010) Funct. Plant Biol. , vol.37 , pp. 1161-1174
    • Wu, L.G.1    Birch, R.G.2
  • 188
    • 34248199965 scopus 로고    scopus 로고
    • Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase
    • doi: 10.1074/jbc.M608310200
    • Wu, Y., Song, P., Xu, J., Zhang, M., and Zou, M. H. (2007). Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase. J. Biol. Chem. 282, 9777-9788. doi: 10.1074/jbc.M608310200
    • (2007) J. Biol. Chem. , vol.282 , pp. 9777-9788
    • Wu, Y.1    Song, P.2    Xu, J.3    Zhang, M.4    Zou, M.H.5
  • 189
    • 34848840368 scopus 로고    scopus 로고
    • Structural basis for AMP binding to mammalian AMP-activated protein kinase
    • doi: 10.1038/nature06161
    • Xiao, B., Heath, R., Saiu, P., Leiper, F. C., Leone, P., Jing, C., et al. (2007). Structural basis for AMP binding to mammalian AMP-activated protein kinase. Nature 449, 496-500. doi: 10.1038/nature06161
    • (2007) Nature , vol.449 , pp. 496-500
    • Xiao, B.1    Heath, R.2    Saiu, P.3    Leiper, F.C.4    Leone, P.5    Jing, C.6
  • 190
    • 79954517977 scopus 로고    scopus 로고
    • Structure of mammalian AMPK and its regulation by ADP
    • doi: 10.1038/nature09932
    • Xiao, B., Sanders, M. J., Underwood, E., Heath, R., Mayer, F. V., Carmena, D., et al. (2011). Structure of mammalian AMPK and its regulation by ADP. Nature 472, 230-233. doi: 10.1038/nature09932
    • (2011) Nature , vol.472 , pp. 230-233
    • Xiao, B.1    Sanders, M.J.2    Underwood, E.3    Heath, R.4    Mayer, F.V.5    Carmena, D.6
  • 191
    • 33751229931 scopus 로고    scopus 로고
    • A pivotal role for endogenous TGF-beta-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway
    • doi: 10.1073/pnas.0604708103
    • Xie, M., Zhang, D., Dyck, J. R., Li, Y., Zhang, H., Morishima, M., et al. (2006). A pivotal role for endogenous TGF-beta-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway. Proc. Natl. Acad. Sci. U.S.A. 103, 17378-17383. doi: 10.1073/pnas.0604708103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17378-17383
    • Xie, M.1    Zhang, D.2    Dyck, J.R.3    Li, Y.4    Zhang, H.5    Morishima, M.6
  • 192
    • 65249160501 scopus 로고    scopus 로고
    • Inhibition of SNF1-related protein kinase1 activity and regulation of metabolic pathways by trehalose-6-phosphate
    • doi: 10.1104/pp.108.133934
    • Zhang, Y., Primavesi, L. F., Jhurreea, D., Andralojc, P. J., Mitchell, R. A., Powers, S. J., et al. (2009). Inhibition of SNF1-related protein kinase1 activity and regulation of metabolic pathways by trehalose-6-phosphate. Plant Physiol. 149, 1860-1871. doi: 10.1104/pp.108.133934
    • (2009) Plant Physiol. , vol.149 , pp. 1860-1871
    • Zhang, Y.1    Primavesi, L.F.2    Jhurreea, D.3    Andralojc, P.J.4    Mitchell, R.A.5    Powers, S.J.6
  • 193
    • 0035543420 scopus 로고    scopus 로고
    • Expression of antisense SnRK1 protein kinase sequence causes abnormal pollen development and male sterility in transgenic barley
    • doi: 10.1046/j.1365-313X.2001.01167.x
    • Zhang, Y., Shewry, P. R., Jones, H., Barcelo, P., Lazzeri, P. A., and Halford, N. G. (2001). Expression of antisense SnRK1 protein kinase sequence causes abnormal pollen development and male sterility in transgenic barley. Plant J. 28, 431-441. doi: 10.1046/j.1365-313X.2001.01167.x
    • (2001) Plant J. , vol.28 , pp. 431-441
    • Zhang, Y.1    Shewry, P.R.2    Jones, H.3    Barcelo, P.4    Lazzeri, P.A.5    Halford, N.G.6
  • 194
    • 84864369594 scopus 로고    scopus 로고
    • Metformin interacts with AMPK through binding to gamma subunit
    • doi: 10.1007/s11010-012-1344-5
    • Zhang, Y., Wang, Y., Bao, C., Xu, Y., Shen, H., Chen, J., et al. (2012). Metformin interacts with AMPK through binding to gamma subunit. Mol. Cell. Biochem. 368, 69-76. doi: 10.1007/s11010-012-1344-5
    • (2012) Mol. Cell. Biochem. , vol.368 , pp. 69-76
    • Zhang, Y.1    Wang, Y.2    Bao, C.3    Xu, Y.4    Shen, H.5    Chen, J.6
  • 195
    • 84885142437 scopus 로고    scopus 로고
    • AMP as a low-energy charge signal autonomously initiates assembly of AXIN-AMPK-LKB1 Complex for AMPK activation
    • doi: 10.1016/j.cmet.2013.09.005
    • Zhang, Y. L., Guo, H., Zhang, C. S., Lin, S. Y., Yin, Z., Peng, Y., et al. (2013). AMP as a low-energy charge signal autonomously initiates assembly of AXIN-AMPK-LKB1 Complex for AMPK activation. Cell Metab. 18, 546-555. doi: 10.1016/j.cmet.2013.09.005
    • (2013) Cell Metab. , vol.18 , pp. 546-555
    • Zhang, Y.L.1    Guo, H.2    Zhang, C.S.3    Lin, S.Y.4    Yin, Z.5    Peng, Y.6
  • 196
    • 0034773404 scopus 로고    scopus 로고
    • Role of AMP-activated protein kinase in mechanism of metformin action
    • doi: 10.1172/JCI13505
    • Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., et al. (2001). Role of AMP-activated protein kinase in mechanism of metformin action. J. Clin. Invest. 108, 1167-1174. doi: 10.1172/JCI13505
    • (2001) J. Clin. Invest. , vol.108 , pp. 1167-1174
    • Zhou, G.1    Myers, R.2    Li, Y.3    Chen, Y.4    Shen, X.5    Fenyk-Melody, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.