PRKAA2

PRKAA2

Protein kinase, AMP-activated, alpha 2 catalytic subunit, also known as PRKAA2, is a human gene.cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene is a catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Hardie DG, MacKintosh RW |title=AMP-activated protein kinase--an archetypal protein kinase cascade? |journal=Bioessays |volume=14 |issue= 10 |pages= 699–704 |year= 1995 |pmid= 1365882 |doi= 10.1002/bies.950141011
*cite journal | author=Hardie DG |title=Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase. |journal=Biochim. Biophys. Acta |volume=1123 |issue= 3 |pages= 231–8 |year= 1992 |pmid= 1536860 |doi=
*cite journal | author=Carling D |title=The AMP-activated protein kinase cascade--a unifying system for energy control. |journal=Trends Biochem. Sci. |volume=29 |issue= 1 |pages= 18–24 |year= 2004 |pmid= 14729328 |doi=
*cite journal | author=Aguan K, Scott J, See CG, Sarkar NH |title=Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals. |journal=Gene |volume=149 |issue= 2 |pages= 345–50 |year= 1994 |pmid= 7959015 |doi=
*cite journal | author=Beri RK, Marley AE, See CG, "et al." |title=Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 117–21 |year= 1995 |pmid= 7988703 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Vavvas D, Apazidis A, Saha AK, "et al." |title=Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13255–61 |year= 1997 |pmid= 9148944 |doi=
*cite journal | author=Stapleton D, Woollatt E, Mitchelhill KI, "et al." |title=AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location. |journal=FEBS Lett. |volume=409 |issue= 3 |pages= 452–6 |year= 1997 |pmid= 9224708 |doi=
*cite journal | author=Stein SC, Woods A, Jones NA, "et al." |title=The regulation of AMP-activated protein kinase by phosphorylation. |journal=Biochem. J. |volume=345 Pt 3 |issue= |pages= 437–43 |year= 2000 |pmid= 10642499 |doi=
*cite journal | author=da Silva Xavier G, Leclerc I, Salt IP, "et al." |title=Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4023–8 |year= 2000 |pmid= 10760274 |doi=
*cite journal | author=Mu J, Brozinick JT, Valladares O, "et al." |title=A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle. |journal=Mol. Cell |volume=7 |issue= 5 |pages= 1085–94 |year= 2001 |pmid= 11389854 |doi=
*cite journal | author=Minokoshi Y, Kim YB, Peroni OD, "et al." |title=Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. |journal=Nature |volume=415 |issue= 6869 |pages= 339–43 |year= 2002 |pmid= 11797013 |doi= 10.1038/415339a
*cite journal | author=Dubbelhuis PF, Meijer AJ |title=Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase. |journal=FEBS Lett. |volume=521 |issue= 1-3 |pages= 39–42 |year= 2002 |pmid= 12067722 |doi=
*cite journal | author=Esumi H, Izuishi K, Kato K, "et al." |title=Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32791–8 |year= 2002 |pmid= 12091379 |doi= 10.1074/jbc.M112270200
*cite journal | author=Nielsen JN, Mustard KJ, Graham DA, "et al." |title=5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle. |journal=J. Appl. Physiol. |volume=94 |issue= 2 |pages= 631–41 |year= 2003 |pmid= 12391032 |doi= 10.1152/japplphysiol.00642.2002
*cite journal | author=Wojtaszewski JF, Mourtzakis M, Hillig T, "et al." |title=Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 3 |pages= 309–16 |year= 2002 |pmid= 12413941 |doi=
*cite journal | author=Hallows KR, McCane JE, Kemp BE, "et al." |title=Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells. |journal=J. Biol. Chem. |volume=278 |issue= 2 |pages= 998–1004 |year= 2003 |pmid= 12427743 |doi= 10.1074/jbc.M210621200
*cite journal | author=Zong H, Ren JM, Young LH, "et al." |title=AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 25 |pages= 15983–7 |year= 2003 |pmid= 12444247 |doi= 10.1073/pnas.252625599

PBB_Controls
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