메뉴 건너뛰기




Volumn 2, Issue 1, 2005, Pages 9-19

Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE; CALCIUM ION; CALCIUM IONOPHORE; CALMODULIN DEPENDENT PROTEIN KINASE KINASE BETA; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; PHOSPHOTRANSFERASE; POTASSIUM ION; PROTEIN KINASE INHIBITOR; PROTEIN KINASE LKB1; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; 5' AMP ACTIVATED PROTEIN KINASE; 5'-AMP-ACTIVATED PROTEIN KINASE; ACETYL COENZYME A CARBOXYLASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BENZIMIDAZOLE DERIVATIVE; CALCIMYCIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE KINASE BETA; CALCIUM CALMODULIN-DEPENDENT PROTEIN KINASE KINASE BETA; ISOQUINOLINE DERIVATIVE; MULTIENZYME COMPLEX; NAPHTHALIMIDE DERIVATIVE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN SERINE THREONINE KINASE; STK11 PROTEIN, MOUSE; STO 609;

EID: 23044432463     PISSN: 15504131     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cmet.2005.05.009     Document Type: Article
Times cited : (1372)

References (48)
  • 1
    • 12844265354 scopus 로고    scopus 로고
    • Myocardial ischemia differentially regulates LKB1 and an alternate 5′-AMP-activated protein kinase kinase
    • J.Y. Altarejos M. Taniguchi A.S. Clanachan G.D. Lopaschuk Myocardial ischemia differentially regulates LKB1 and an alternate 5′-AMP-activated protein kinase kinase J. Biol. Chem. 280 2005 183-190
    • (2005) J. Biol. Chem. , vol.280 , pp. 183-190
    • Altarejos, J.Y.1    Taniguchi, M.2    Clanachan, A.S.3    Lopaschuk, G.D.4
  • 3
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • J. Bain H. McLauchlan M. Elliott P. Cohen The specificities of protein kinase inhibitors: An update Biochem. J. 371 2003 199-204
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 5
    • 0031016272 scopus 로고    scopus 로고
    • The structure of a domain common to archaebacteria and the homocystinuria disease protein
    • A. Bateman The structure of a domain common to archaebacteria and the homocystinuria disease protein Trends Biochem. Sci. 22 1997 12-13
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 12-13
    • Bateman, A.1
  • 6
    • 0347318052 scopus 로고    scopus 로고
    • The AMP-activated protein kinase cascade - A unifying system for energy control
    • D. Carling The AMP-activated protein kinase cascade - a unifying system for energy control Trends Biochem. Sci. 29 2004 18-24
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 18-24
    • Carling, D.1
  • 8
    • 0034803430 scopus 로고    scopus 로고
    • AMP-activated protein kinase is highly expressed in neurons in the developing rat brain and promotes neuronal survival following glucose deprivation
    • C. Culmsee J. Monnig B.E. Kemp M.P. Mattson AMP-activated protein kinase is highly expressed in neurons in the developing rat brain and promotes neuronal survival following glucose deprivation J. Mol. Neurosci. 17 2001 45-58
    • (2001) J. Mol. Neurosci. , vol.17 , pp. 45-58
    • Culmsee, C.1    Monnig, J.2    Kemp, B.E.3    Mattson, M.P.4
  • 9
    • 0024839973 scopus 로고
    • Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic AMP-dependent protein kinase, studied using a specific and sensitive peptide assay
    • S.P. Davies D. Carling D.G. Hardie Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic AMP-dependent protein kinase, studied using a specific and sensitive peptide assay Eur. J. Biochem. 186 1989 123-128
    • (1989) Eur. J. Biochem. , vol.186 , pp. 123-128
    • Davies, S.P.1    Carling, D.2    Hardie, D.G.3
  • 11
    • 0034614420 scopus 로고    scopus 로고
    • Dimethylbiguanide inhibits cell respiration via an indirect effect targeted on the respiratory chain complex I
    • M.Y. El-Mir V. Nogueira E. Fontaine N. Averet M. Rigoulet X. Leverve Dimethylbiguanide inhibits cell respiration via an indirect effect targeted on the respiratory chain complex I J. Biol. Chem. 275 2000 223-228
    • (2000) J. Biol. Chem. , vol.275 , pp. 223-228
    • El-Mir, M.Y.1    Nogueira, V.2    Fontaine, E.3    Averet, N.4    Rigoulet, M.5    Leverve, X.6
  • 12
    • 0028782748 scopus 로고
    • Block of neuronal apoptosis by a sustained increase of steady-state free Ca2+ concentration
    • J.L. Franklin E.M. Johnson Jr. Block of neuronal apoptosis by a sustained increase of steady-state free Ca2+ concentration Philos. Trans. R. Soc. Lond. B Biol. Sci. 345 1994 251-256
    • (1994) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.345 , pp. 251-256
    • Franklin, J.L.1    Johnson Jr., E.M.2
  • 13
    • 0037067666 scopus 로고    scopus 로고
    • The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct pathways
    • L.G. Fryer A. Parbu-Patel D. Carling The anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct pathways J. Biol. Chem. 277 2002 25226-25232
    • (2002) J. Biol. Chem. , vol.277 , pp. 25226-25232
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 14
    • 10744230942 scopus 로고    scopus 로고
    • Distinct mechanisms underlie the activation of rat brain AMP-activated protein kinase and the inhibition of excitatory synaptic transmission by AICA riboside (Acadesine) in area CA1 of rat hippocampus
    • A.E. Gadalla T. Pearson A.J. Currie N. Dale S.A. Hawley A.D. Randall D.G. Hardie B.G. Frenguelli Distinct mechanisms underlie the activation of rat brain AMP-activated protein kinase and the inhibition of excitatory synaptic transmission by AICA riboside (Acadesine) in area CA1 of rat hippocampus J. Neurochem. 88 2004 1272-1282
    • (2004) J. Neurochem. , vol.88 , pp. 1272-1282
    • Gadalla, A.E.1    Pearson, T.2    Currie, A.J.3    Dale, N.4    Hawley, S.A.5    Randall, A.D.6    Hardie, D.G.7    Frenguelli, B.G.8
  • 15
    • 10944247187 scopus 로고    scopus 로고
    • The AMP-activated protein kinase pathway - New players upstream and downstream
    • D.G. Hardie The AMP-activated protein kinase pathway - new players upstream and downstream J. Cell Sci. 117 2004 5479-5487
    • (2004) J. Cell Sci. , vol.117 , pp. 5479-5487
    • Hardie, D.G.1
  • 16
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase: The energy charge hypothesis revisited
    • D.G. Hardie S.A. Hawley AMP-activated protein kinase: The energy charge hypothesis revisited Bioessays 23 2001 1112-1119
    • (2001) Bioessays , vol.23 , pp. 1112-1119
    • Hardie, D.G.1    Hawley, S.A.2
  • 17
    • 0033560109 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An ultrasensitive system for monitoring cellular energy charge
    • D.G. Hardie I.P. Salt S.A. Hawley S.P. Davies AMP-activated protein kinase: An ultrasensitive system for monitoring cellular energy charge Biochem. J. 338 1999 717-722
    • (1999) Biochem. J. , vol.338 , pp. 717-722
    • Hardie, D.G.1    Salt, I.P.2    Hawley, S.A.3    Davies, S.P.4
  • 18
    • 0038199737 scopus 로고    scopus 로고
    • Management of cellular energy by the AMP-activated protein kinase system
    • D.G. Hardie J.W. Scott D.A. Pan E.R. Hudson Management of cellular energy by the AMP-activated protein kinase system FEBS Lett. 546 2003 113-120
    • (2003) FEBS Lett. , vol.546 , pp. 113-120
    • Hardie, D.G.1    Scott, J.W.2    Pan, D.A.3    Hudson, E.R.4
  • 20
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase
    • S.A. Hawley M. Davison A. Woods S.P. Davies R.K. Beri D. Carling D.G. Hardie Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase J. Biol. Chem. 271 1996 27879-27887
    • (1996) J. Biol. Chem. , vol.271 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 21
    • 0036324142 scopus 로고    scopus 로고
    • The anti-diabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism
    • S.A. Hawley A.E. Gadalla G.S. Olsen D.G. Hardie The anti-diabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism Diabetes 51 2002 2420-2425
    • (2002) Diabetes , vol.51 , pp. 2420-2425
    • Hawley, S.A.1    Gadalla, A.E.2    Olsen, G.S.3    Hardie, D.G.4
  • 22
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade
    • S.A. Hawley J. Boudeau J.L. Reid K.J. Mustard L. Udd T.P. Makela D.R. Alessi D.G. Hardie Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade J. Biol. 2 2003 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    Alessi, D.R.7    Hardie, D.G.8
  • 23
    • 0041305909 scopus 로고    scopus 로고
    • Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases
    • S.P. Hong F.C. Leiper A. Woods D. Carling M. Carlson Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases Proc. Natl. Acad. Sci. USA 100 2003 8839-8843
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8839-8843
    • Hong, S.P.1    Leiper, F.C.2    Woods, A.3    Carling, D.4    Carlson, M.5
  • 24
    • 0038814313 scopus 로고    scopus 로고
    • A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias
    • E.R. Hudson D.A. Pan J. James J.M. Lucocq S.A. Hawley K.A. Green O. Baba T. Terashima D.G. Hardie A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias Curr. Biol. 13 2003 861-866
    • (2003) Curr. Biol. , vol.13 , pp. 861-866
    • Hudson, E.R.1    Pan, D.A.2    James, J.3    Lucocq, J.M.4    Hawley, S.A.5    Green, K.A.6    Baba, O.7    Terashima, T.8    Hardie, D.G.9
  • 25
    • 0142039017 scopus 로고    scopus 로고
    • Identification and characterization of novel components of a Ca2+/ calmodulin-dependent protein kinase cascade in HeLa cells
    • Y. Ishikawa H. Tokumitsu H. Inuzuka M. Murata-Hori H. Hosoya R. Kobayashi Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells FEBS Lett. 550 2003 57-63
    • (2003) FEBS Lett. , vol.550 , pp. 57-63
    • Ishikawa, Y.1    Tokumitsu, H.2    Inuzuka, H.3    Murata-Hori, M.4    Hosoya, H.5    Kobayashi, R.6
  • 26
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism
    • B.B. Kahn T. Alquier D. Carling D.G. Hardie AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism Cell Metab. 1 2005 15-25
    • (2005) Cell Metab. , vol.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 27
    • 1342332128 scopus 로고    scopus 로고
    • Bateman domains and adenosine derivatives form a binding contract
    • B.E. Kemp Bateman domains and adenosine derivatives form a binding contract J. Clin. Invest. 113 2004 182-184
    • (2004) J. Clin. Invest. , vol.113 , pp. 182-184
    • Kemp, B.E.1
  • 28
    • 9444249257 scopus 로고    scopus 로고
    • AMP-activated protein kinase: A new beta-cell glucose sensor? Regulation by amino acids and calcium ions
    • I. Leclerc G.A. Rutter AMP-activated protein kinase: A new beta-cell glucose sensor? Regulation by amino acids and calcium ions Diabetes Suppl. 3 53 2004 S67-S74
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 3
    • Leclerc, I.1    Rutter, G.A.2
  • 30
    • 0037335465 scopus 로고    scopus 로고
    • Homeostatic effects of depolarization on Ca2+ influx, synaptic signaling, and survival
    • K.L. Moulder R.J. Cormier A.A. Shute C.F. Zorumski S. Mennerick Homeostatic effects of depolarization on Ca2+ influx, synaptic signaling, and survival J. Neurosci. 23 2003 1825-1831
    • (2003) J. Neurosci. , vol.23 , pp. 1825-1831
    • Moulder, K.L.1    Cormier, R.J.2    Shute, A.A.3    Zorumski, C.F.4    Mennerick, S.5
  • 31
    • 18744432273 scopus 로고
    • Towards the molecular basis for the regulation of mitochondrial dehydrogenases by calcium ions
    • B.J. Nichols R.M. Denton Towards the molecular basis for the regulation of mitochondrial dehydrogenases by calcium ions Mol. Cell. Biochem. 149-150 1995 203-212
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 203-212
    • Nichols, B.J.1    Denton, R.M.2
  • 32
    • 0034659785 scopus 로고    scopus 로고
    • Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain
    • M.R. Owen E. Doran A.P. Halestrap Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain Biochem. J. 348 2000 607-614
    • (2000) Biochem. J. , vol.348 , pp. 607-614
    • Owen, M.R.1    Doran, E.2    Halestrap, A.P.3
  • 34
    • 20044370885 scopus 로고    scopus 로고
    • Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction
    • K. Sakamoto A. McCarthy D. Smith K.A. Green D.G. Hardie A. Ashworth D.R. Alessi Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction EMBO J. 24 2005 1810-1820
    • (2005) EMBO J. , vol.24 , pp. 1810-1820
    • Sakamoto, K.1    McCarthy, A.2    Smith, D.3    Green, K.A.4    Hardie, D.G.5    Ashworth, A.6    Alessi, D.R.7
  • 36
    • 3042611866 scopus 로고    scopus 로고
    • A calmodulin-regulated protein kinase linked to neuron survival is a substrate for the calmodulin-regulated death-associated protein kinase
    • A.M. Schumacher J.P. Schavocky A.V. Velentza S. Mirzoeva D.M. Watterson A calmodulin-regulated protein kinase linked to neuron survival is a substrate for the calmodulin-regulated death-associated protein kinase Biochemistry 43 2004 8116-8124
    • (2004) Biochemistry , vol.43 , pp. 8116-8124
    • Schumacher, A.M.1    Schavocky, J.P.2    Velentza, A.V.3    Mirzoeva, S.4    Watterson, D.M.5
  • 37
    • 0036290846 scopus 로고    scopus 로고
    • Protein kinase substrate recognition studied using the recombinant catalytic domain of AMP-activated protein kinase and a model substrate
    • J.W. Scott D.G. Norman S.A. Hawley L. Kontogiannis D.G. Hardie Protein kinase substrate recognition studied using the recombinant catalytic domain of AMP-activated protein kinase and a model substrate J. Mol. Biol. 317 2002 309-323
    • (2002) J. Mol. Biol. , vol.317 , pp. 309-323
    • Scott, J.W.1    Norman, D.G.2    Hawley, S.A.3    Kontogiannis, L.4    Hardie, D.G.5
  • 40
    • 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
    • C. Sugden R.M. Crawford N.G. Halford D.G. Hardie 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 1999 433-439
    • (1999) Plant J. , vol.19 , pp. 433-439
    • Sugden, C.1    Crawford, R.M.2    Halford, N.G.3    Hardie, D.G.4
  • 42
    • 0033529838 scopus 로고    scopus 로고
    • Growth suppression by LKB1 is mediated by a G(1) cell cycle arrest
    • M. Tiainen A. Ylikorkala T.P. Makela Growth suppression by LKB1 is mediated by a G(1) cell cycle arrest Proc. Natl. Acad. Sci. USA 96 1999 9248-9251
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9248-9251
    • Tiainen, M.1    Ylikorkala, A.2    Makela, T.P.3
  • 45
    • 0029978799 scopus 로고    scopus 로고
    • Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise
    • W.W. Winder D.G. Hardie Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise Am. J. Physiol. 270 1996 E299-E304
    • (1996) Am. J. Physiol. , vol.270
    • Winder, W.W.1    Hardie, D.G.2
  • 46
    • 0030592623 scopus 로고    scopus 로고
    • The α1 and α2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro
    • A. Woods I. Salt J. Scott D.G. Hardie D. Carling The α1 and α2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro FEBS Lett. 397 1996 347-351
    • (1996) FEBS Lett. , vol.397 , pp. 347-351
    • Woods, A.1    Salt, I.2    Scott, J.3    Hardie, D.G.4    Carling, D.5
  • 48
    • 0032506514 scopus 로고    scopus 로고
    • Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway
    • S. Yano H. Tokumitsu T.R. Soderling Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway Nature 396 1998 584-587
    • (1998) Nature , vol.396 , pp. 584-587
    • Yano, S.1    Tokumitsu, H.2    Soderling, T.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.