KEGG   PATHWAY: ocu04152
Entry
ocu04152                    Pathway                                
Name
AMPK signaling pathway - Oryctolagus cuniculus (rabbit)
Description
AMP-activated protein kinase (AMPK) is a serine threonine kinase that is highly conserved through evolution. AMPK system acts as a sensor of cellular energy status. It is activated by increases in the cellular AMP:ATP ratio caused by metabolic stresses that either interfere with ATP production (eg, deprivation for glucose or oxygen) or that accelerate ATP consumption (eg, muscle contraction). Several upstream kinases, including liver kinase B1 (LKB1), calcium/calmodulin kinase kinase-beta (CaMKK beta), and TGF-beta-activated kinase-1 (TAK-1), can activate AMPK by phosphorylating a threonine residue on its catalytic alpha-subunit. Once activated, AMPK leads to a concomitant inhibition of energy-consuming biosynthetic pathways, such as protein, fatty acid and glycogen synthesis, and activation of ATP-producing catabolic pathways, such as fatty acid oxidation and glycolysis.
Class
Environmental Information Processing; Signal transduction
Pathway map
ocu04152  AMPK signaling pathway
ocu04152

Other DBs
GO: 2000479
Organism
Oryctolagus cuniculus (rabbit) [GN:ocu]
Gene
100008660  GYS1; glycogen [starch] synthase, muscle [KO:K00693] [EC:2.4.1.11]
100008668  IGF1; insulin-like growth factor I precursor [KO:K05459]
100008747  LEP; leptin precursor [KO:K05424]
100008825  [KO:K06259]
100008853  FBP2; fructose-1,6-bisphosphatase isozyme 2 [KO:K03841] [EC:3.1.3.11]
100008863  [KO:K03841] [EC:3.1.3.11]
100008892  PPARG; peroxisome proliferator-activated receptor gamma [KO:K08530]
100008911  [KO:K04527] [EC:2.7.10.1]
100009027  ADIPOQ; adiponectin precursor [KO:K07296]
100009139  PPP2R2B; serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform [KO:K04354]
100009215  PPP2R5B; serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform [KO:K11584]
100009216  PPP2R5C; serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform [KO:K11584]
100009237  ADRA1A; alpha-1A adrenergic receptor [KO:K04135]
100009252  PPP2CA; serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform [KO:K04382] [EC:3.1.3.16]
100009260  RPS6KB1; ribosomal protein S6 kinase beta-1 [KO:K04688] [EC:2.7.11.1]
100009281  RAB2A; ras-related protein Rab-2A [KO:K07877]
100009300  PPP2CB; serine/threonine-protein phosphatase 2A catalytic subunit beta isoform [KO:K04382] [EC:3.1.3.16]
100009434  [KO:K11584]
100009471  CFTR; cystic fibrosis transmembrane conductance regulator [KO:K05031] [EC:5.6.1.6]
100009526  PFKP; ATP-dependent 6-phosphofructokinase, platelet type [KO:K00850] [EC:2.7.1.11]
100009533  PPP2R5D; serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform [KO:K11584]
100037710  SLC2A4; solute carrier family 2, facilitated glucose transporter member 4 [KO:K07191]
100134866  CCNA2; cyclin-A2 [KO:K06627]
100144331  [KO:K07297]
100144332  [KO:K07297]
100144341  [KO:K01596] [EC:4.1.1.32]
100144342  [KO:K05087] [EC:2.7.10.1]
100303766  G6PC1; glucose-6-phosphatase catalytic subunit 1 [KO:K01084] [EC:3.1.3.9]
100328616  PPP2R2A; serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform [KO:K04354]
100328617  PPP2R2C; serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform [KO:K04354]
100337822  [KO:K00922] [EC:2.7.1.153]
100338228  [KO:K01578] [EC:4.1.1.9]
100338597  [KO:K07881]
100338695  [KO:K07206]
100338850  [KO:K07205]
100339305  [KO:K17445]
100339362  [KO:K01946] [EC:6.4.1.2 6.3.4.14 2.1.3.15]
100339941  [KO:K07188] [EC:3.1.1.79]
100339981  [KO:K16172]
100340412  [KO:K07199]
100340670  [KO:K07198] [EC:2.7.11.31]
100341327  [KO:K19524] [EC:2.3.1.21]
100342118  [KO:K08272]
100342852  [KO:K04456] [EC:2.7.11.1]
100342882  [KO:K17532]
100343130  [KO:K09048]
100343571  [KO:K04427] [EC:2.7.11.25]
100343573  [KO:K09408]
100344174  [KO:K19029] [EC:2.7.1.105 3.1.3.46]
100344498  [KO:K00507] [EC:1.14.19.1]
100345023  [KO:K19028] [EC:2.7.1.105 3.1.3.46]
100345181  [KO:K00922] [EC:2.7.1.153]
100345242  [KO:K19030] [EC:2.7.1.105 3.1.3.46]
100345250  [KO:K02649]
100345457  [KO:K07292]
100345475  [KO:K09048]
100345647  [KO:K00850] [EC:2.7.1.11]
100345755  [KO:K01084] [EC:3.1.3.9]
100346046  [KO:K00507] [EC:1.14.19.1]
100346306  [KO:K00507] [EC:1.14.19.1]
100346561  [KO:K00507] [EC:1.14.19.1]
100346997  [KO:K11584]
100347318  [KO:K25893]
100347896  [KO:K08292] [EC:2.7.11.20]
100347954  [KO:K06276] [EC:2.7.11.1]
100348286  [KO:K04354]
100348492  [KO:K07208]
100348595  [KO:K08271]
100348663  [KO:K00922] [EC:2.7.1.153]
100348780  [KO:K07199]
100349219  [KO:K07202]
100349271  [KO:K11411] [EC:2.3.1.286]
100350311  [KO:K08765] [EC:2.3.1.21]
100350534  [KO:K01103] [EC:2.7.1.105 3.1.3.46]
100350689  [KO:K07359] [EC:2.7.11.17]
100350716  [KO:K08765] [EC:2.3.1.21]
100350803  [KO:K21357] [EC:2.7.11.1]
100351640  [KO:K07207]
100351924  [KO:K05062]
100351999  [KO:K05870]
100352581  [KO:K07200]
100352741  [KO:K18341]
100352785  [KO:K06627]
100352840  [KO:K00693] [EC:2.4.1.11]
100353138  [KO:K19523] [EC:2.3.1.21]
100353180  [KO:K07200]
100353220  ELAVL1; ELAV-like protein 1 [KO:K13088]
100353545  [KO:K11583]
100353706  [KO:K04456] [EC:2.7.11.1]
100355092  [KO:K03456]
100355159  [KO:K11583]
100355357  [KO:K07903]
100355758  [KO:K03456]
100355970  [KO:K11262] [EC:6.4.1.2 6.3.4.14 2.1.3.15]
100356164  [KO:K07203] [EC:2.7.11.1]
100356542  [KO:K07200]
100356580  [KO:K11583]
100357419  [KO:K00507] [EC:1.14.19.1]
100357483  [KO:K09047]
100357791  [KO:K00021] [EC:1.1.1.34]
100357841  [KO:K02649]
100357876  [KO:K09048]
100358166  [KO:K07198] [EC:2.7.11.31]
100358175  [KO:K09048]
100358389  [KO:K06627]
100358467  [KO:K08272]
100358471  [KO:K07201]
100358563  [KO:K07905]
100358721  [KO:K01084] [EC:3.1.3.9]
100358960  [KO:K16333]
103345363  [KO:K07901]
103346501  [KO:K07197]
103346553  [KO:K07204]
103346593  [KO:K08765] [EC:2.3.1.21]
103347367  [KO:K00850] [EC:2.7.1.11]
103349113  [KO:K07187]
103351932  [KO:K17446]
127482593  [KO:K07877]
127482734  [KO:K07204]
127484730  [KO:K04688] [EC:2.7.11.1]
127485698  [KO:K03234]
127486116  [KO:K04456] [EC:2.7.11.1]
127488422  [KO:K07359] [EC:2.7.11.17]
127489204  [KO:K07298] [EC:2.7.11.1]
127489858  [KO:K16184]
Compound
C00003  NAD+
C00008  ADP
C00020  AMP
C00022  Pyruvate
C00024  Acetyl-CoA
C00031  D-Glucose
C00040  Acyl-CoA
C00076  Calcium cation
C00083  Malonyl-CoA
C00085  D-Fructose 6-phosphate
C00162  Fatty acid
C00354  D-Fructose 1,6-bisphosphate
C00389  Quercetin
C00665  beta-D-Fructose 2,6-bisphosphate
C00668  alpha-D-Glucose 6-phosphate
C00698  Cl-
C00757  Berberine
C01172  beta-D-Glucose 6-phosphate
C04677  1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide
C05981  Phosphatidylinositol-3,4,5-trisphosphate
C07151  Metformin
C09731  Epigallocatechin gallate
D08351  Phenformin (BAN)
Reference
  Authors
Steinberg GR, Kemp BE
  Title
AMPK in Health and Disease.
  Journal
Physiol Rev 89:1025-78 (2009)
DOI:10.1152/physrev.00011.2008
Reference
  Authors
Hardie DG.
  Title
The AMP-activated protein kinase pathway--new players upstream and downstream.
  Journal
J Cell Sci 117:5479-87 (2004)
DOI:10.1242/jcs.01540
Reference
  Authors
Russo GL, Russo M, Ungaro P
  Title
AMP-activated protein kinase: a target for old drugs against diabetes and cancer.
  Journal
Biochem Pharmacol 86:339-50 (2013)
DOI:10.1016/j.bcp.2013.05.023
Reference
  Authors
Ronnett GV, Ramamurthy S, Kleman AM, Landree LE, Aja S
  Title
AMPK in the brain: its roles in energy balance and neuroprotection.
  Journal
J Neurochem 109 Suppl 1:17-23 (2009)
DOI:10.1111/j.1471-4159.2009.05916.x
Reference
  Authors
Li J, McCullough LD
  Title
Effects of AMP-activated protein kinase in cerebral ischemia.
  Journal
J Cereb Blood Flow Metab 30:480-92 (2010)
DOI:10.1038/jcbfm.2009.255
Reference
  Authors
Sanchez AM, Candau RB, Csibi A, Pagano AF, Raibon A, Bernardi H
  Title
The role of AMP-activated protein kinase in the coordination of skeletal muscle turnover and energy homeostasis.
  Journal
Am J Physiol Cell Physiol 303:C475-85 (2012)
DOI:10.1152/ajpcell.00125.2012
Reference
  Authors
Viollet B, Foretz M, Guigas B, Horman S, Dentin R, Bertrand L, Hue L, Andreelli F
  Title
Activation of AMP-activated protein kinase in the liver: a new strategy for the management of metabolic hepatic disorders.
  Journal
J Physiol 574:41-53 (2006)
DOI:10.1113/jphysiol.2006.108506
Reference
  Authors
Shackelford DB, Shaw RJ
  Title
The LKB1-AMPK pathway: metabolism and growth control in tumour suppression.
  Journal
Nat Rev Cancer 9:563-75 (2009)
DOI:10.1038/nrc2676
Reference
  Authors
Chung JH, Manganiello V, Dyck JR
  Title
Resveratrol as a calorie restriction mimetic: therapeutic implications.
  Journal
Trends Cell Biol 22:546-54 (2012)
DOI:10.1016/j.tcb.2012.07.004
Reference
  Authors
Iwabu M, Yamauchi T, Okada-Iwabu M, Sato K, Nakagawa T, Funata M, Yamaguchi M, Namiki S, Nakayama R, Tabata M, Ogata H, Kubota N, Takamoto I, Hayashi YK, Yamauchi N, Waki H, Fukayama M, Nishino I, Tokuyama K, Ueki K, Oike Y, Ishii S, Hirose K, Shimizu T, Touhara K, Kadowaki T
  Title
Adiponectin and AdipoR1 regulate PGC-1alpha and mitochondria by Ca(2+) and AMPK/SIRT1.
  Journal
Nature 464:1313-9 (2010)
DOI:10.1038/nature08991
Reference
  Authors
Towler MC, Hardie DG
  Title
AMP-activated protein kinase in metabolic control and insulin signaling.
  Journal
Circ Res 100:328-41 (2007)
DOI:10.1161/01.RES.0000256090.42690.05
Reference
  Authors
Richter EA, Hargreaves M
  Title
Exercise, GLUT4, and skeletal muscle glucose uptake.
  Journal
Physiol Rev 93:993-1017 (2013)
DOI:10.1152/physrev.00038.2012
Reference
  Authors
Kahn BB, Alquier T, Carling D, Hardie DG
  Title
AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism.
  Journal
Cell Metab 1:15-25 (2005)
DOI:10.1016/j.cmet.2004.12.003
Reference
  Authors
Minokoshi Y, Toda C, Okamoto S
  Title
Regulatory role of leptin in glucose and lipid metabolism in skeletal muscle.
  Journal
Indian J Endocrinol Metab 16:S562-8 (2012)
DOI:10.4103/2230-8210.105573
Reference
  Authors
Guggino WB, Stanton BA
  Title
New insights into cystic fibrosis: molecular switches that regulate CFTR.
  Journal
Nat Rev Mol Cell Biol 7:426-36 (2006)
DOI:10.1038/nrm1949
Reference
  Authors
Cheng A, Saltiel AR
  Title
More TORC for the gluconeogenic engine.
  Journal
Bioessays 28:231-4 (2006)
DOI:10.1002/bies.20375
Reference
  Authors
Herrero-Martin G, Hoyer-Hansen M, Garcia-Garcia C, Fumarola C, Farkas T, Lopez-Rivas A, Jaattela M
  Title
TAK1 activates AMPK-dependent cytoprotective autophagy in TRAIL-treated epithelial cells.
  Journal
EMBO J 28:677-85 (2009)
DOI:10.1038/emboj.2009.8
Reference
  Authors
Morris DL, Rui L
  Title
Recent advances in understanding leptin signaling and leptin resistance.
  Journal
Am J Physiol Endocrinol Metab 297:E1247-59 (2009)
DOI:10.1152/ajpendo.00274.2009
Reference
  Authors
Minokoshi Y, Shiuchi T, Lee S, Suzuki A, Okamoto S
  Title
Role of hypothalamic AMP-kinase in food intake regulation.
  Journal
Nutrition 24:786-90 (2008)
DOI:10.1016/j.nut.2008.06.002
Reference
  Authors
Miyamoto L, Ebihara K, Kusakabe T, Aotani D, Yamamoto-Kataoka S, Sakai T, Aizawa-Abe M, Yamamoto Y, Fujikura J, Hayashi T, Hosoda K, Nakao K
  Title
Leptin activates hepatic 5'-AMP-activated protein kinase through sympathetic nervous system and alpha1-adrenergic receptor: a potential mechanism for improvement of fatty liver in lipodystrophy by leptin.
  Journal
J Biol Chem 287:40441-7 (2012)
DOI:10.1074/jbc.M112.384545
Related
pathway
ocu00010  Glycolysis / Gluconeogenesis
ocu00061  Fatty acid biosynthesis
ocu00500  Starch and sucrose metabolism
ocu01040  Biosynthesis of unsaturated fatty acids
ocu04110  Cell cycle
ocu04140  Autophagy - animal
ocu04150  mTOR signaling pathway
ocu04151  PI3K-Akt signaling pathway
ocu04910  Insulin signaling pathway
ocu04920  Adipocytokine signaling pathway
KO pathway
ko04152   

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