Biology:PRKAA2
Generic protein structure example |
5'-AMP-activated protein kinase catalytic subunit alpha-2 is an enzyme that in humans is encoded by the PRKAA2 gene.[1][2]
Function
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.[2]
References
- ↑ "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. Dec 1994. doi:10.1016/0378-1119(94)90174-0. PMID 7959015.
- ↑ 2.0 2.1 "Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563.
Further reading
- "AMP-activated protein kinase--an archetypal protein kinase cascade?". BioEssays 14 (10): 699–704. 1995. doi:10.1002/bies.950141011. PMID 1365882.
- "Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase". Biochim. Biophys. Acta 1123 (3): 231–8. 1992. doi:10.1016/0005-2760(92)90001-c. PMID 1536860.
- "The AMP-activated protein kinase cascade--a unifying system for energy control". Trends Biochem. Sci. 29 (1): 18–24. 2004. doi:10.1016/j.tibs.2003.11.005. PMID 14729328.
- "Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase". FEBS Lett. 356 (1): 117–21. 1995. doi:10.1016/0014-5793(94)01247-4. PMID 7988703.
- "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. 1997. doi:10.1101/gr.6.9.791. PMID 8889548.
- "Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle". J. Biol. Chem. 272 (20): 13255–61. 1997. doi:10.1074/jbc.272.20.13255. PMID 9148944.
- "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location". FEBS Lett. 409 (3): 452–6. 1997. doi:10.1016/S0014-5793(97)00569-3. PMID 9224708.
- "The regulation of AMP-activated protein kinase by phosphorylation". Biochem. J. 345 (3): 437–43. 2000. doi:10.1042/0264-6021:3450437. PMID 10642499.
- "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. 2000. doi:10.1073/pnas.97.8.4023. PMID 10760274. Bibcode: 2000PNAS...97.4023D.
- "A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle". Mol. Cell 7 (5): 1085–94. 2001. doi:10.1016/S1097-2765(01)00251-9. PMID 11389854.
- "Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase". Nature 415 (6869): 339–43. 2002. doi:10.1038/415339a. PMID 11797013. Bibcode: 2002Natur.415..339M.
- "Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase". FEBS Lett. 521 (1–3): 39–42. 2002. doi:10.1016/S0014-5793(02)02815-6. PMID 12067722.
- "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. 2002. doi:10.1074/jbc.M112270200. PMID 12091379.
- "5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle". J. Appl. Physiol. 94 (2): 631–41. 2003. doi:10.1152/japplphysiol.00642.2002. PMID 12391032.
- "Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise". Biochem. Biophys. Res. Commun. 298 (3): 309–16. 2002. doi:10.1016/S0006-291X(02)02465-8. PMID 12413941.
- "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. 2003. doi:10.1074/jbc.M210621200. PMID 12427743.
- "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. 2003. doi:10.1073/pnas.252625599. PMID 12444247.
Original source: https://en.wikipedia.org/wiki/PRKAA2.
Read more |