PRKAA2

From Wikipedia, the free encyclopedia

Protein kinase, AMP-activated, alpha 2 catalytic subunit

PDB rendering based on 2h6d.

Available structures: 2h6d

Identifiers

Symbol(s)

PRKAA2; AMPK; AMPK2; PRKAA

External IDs

OMIM: 600497 MGI: 1336173 HomoloGene: 4551

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • ATP binding • transferase activity
Cellular Component:	• nucleus
Biological Process:	• protein amino acid phosphorylation • fatty acid biosynthetic process • cholesterol biosynthetic process • signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006252 (mRNA)
NP_006243 (protein)

NM_178143 (mRNA)
NP_835279 (protein)

Location

Chr 1: 56.88 - 56.95 Mb

Chr 4: 104.53 - 104.61 Mb

Pubmed search

[1]

[2]

Protein kinase, AMP-activated, alpha 2 catalytic subunit, also known as PRKAA2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit.

[edit] Further reading

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