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PRKAA2
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<h2 id="function">Function</h2> <p>The <a href="/facts/Protein/Jxmagu3E">protein</a> encoded by this gene is a catalytic subunit of the <a href="/facts/AMP-activated_protein_kinase/Uka4mXB7">AMP-activated protein kinase</a> (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 <a href="/facts/Phosphorylation/LXUEEeIL">phosphorylates</a> and inactivates <a href="/facts/Acetyl-CoA_carboxylase/9Lh10Lrs">acetyl-CoA carboxylase</a> (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (<a href="/facts/HMG-CoA_reductase/F6xSdUIt">HMGCR</a>), key enzymes involved in regulating de novo <a href="/facts/Biosynthesis/aFk7Tk7f">biosynthesis</a> of <a href="/facts/Fatty_acid/JGg3erIu">fatty acid</a> and <a href="/facts/Cholesterol/TnfPlYc1">cholesterol</a>. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body <a href="/facts/Insulin/oXG0myt1">insulin</a> sensitivity and is necessary for maintaining myocardial energy homeostasis during <a href="/facts/Ischemia/ySL9xbCl">ischemia</a>.<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> </p> <h2 id="further-reading">Further reading</h2> <ul><li>Hardie DG, MacKintosh RW (1995). "AMP-activated protein kinase--an archetypal protein kinase cascade?". <i>BioEssays</i>. 14 (10): 699–704. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fbies.950141011">10.1002/bies.950141011</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1365882">1365882</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:37111181">37111181</a>.</li> <li>Hardie DG (1992). "Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase". <i>Biochim. Biophys. Acta</i>. 1123 (3): 231–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0005-2760%2892%2990001-c">10.1016/0005-2760(92)90001-c</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1536860">1536860</a>.</li> <li>Carling D (2004). "The AMP-activated protein kinase cascade--a unifying system for energy control". <i>Trends Biochem. Sci</i>. 29 (1): 18–24. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.tibs.2003.11.005">10.1016/j.tibs.2003.11.005</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14729328">14729328</a>.</li> <li>Beri RK, Marley AE, See CG, Sopwith WF, Aguan K, Carling D, Scott J, Carey F (1995). <a href="https://doi.org/10.1016%2F0014-5793%2894%2901247-4">"Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase"</a>. <i>FEBS Lett</i>. 356 (1): 117–21. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0014-5793%2894%2901247-4">10.1016/0014-5793(94)01247-4</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7988703">7988703</a>.</li> <li>Bonaldo MF, Lennon G, Soares MB (1997). <a href="https://doi.org/10.1101%2Fgr.6.9.791">"Normalization and subtraction: two approaches to facilitate gene discovery"</a>. <i>Genome Res</i>. 6 (9): 791–806. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1101%2Fgr.6.9.791">10.1101/gr.6.9.791</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8889548">8889548</a>.</li> <li>Vavvas D, Apazidis A, Saha AK, Gamble J, Patel A, Kemp BE, Witters LA, Ruderman NB (1997). <a href="https://doi.org/10.1074%2Fjbc.272.20.13255">"Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle"</a>. <i>J. Biol. Chem</i>. 272 (20): 13255–61. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.272.20.13255">10.1074/jbc.272.20.13255</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9148944">9148944</a>.</li> <li>Stapleton D, Woollatt E, Mitchelhill KI, Nicholl JK, Fernandez CS, Michell BJ, Witters LA, Power DA, <a href="/facts/Grant_Robert_Sutherland/sywvNzqT">Sutherland GR</a>, Kemp BE (1997). "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location". <i>FEBS Lett</i>. 409 (3): 452–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0014-5793%2897%2900569-3">10.1016/S0014-5793(97)00569-3</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9224708">9224708</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:39329574">39329574</a>.</li> <li>Stein SC, Woods A, Jones NA, Davison MD, Carling D (2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220775">"The regulation of AMP-activated protein kinase by phosphorylation"</a>. <i>Biochem. J</i>. 345 (3): 437–43. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1042%2F0264-6021%3A3450437">10.1042/0264-6021:3450437</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220775">1220775</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10642499">10642499</a>.</li> <li>da Silva Xavier G, Leclerc I, Salt IP, Doiron B, Hardie DG, Kahn A, Rutter GA (2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC18135">"Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 97 (8): 4023–8. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2000PNAS...97.4023D">2000PNAS...97.4023D</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.97.8.4023">10.1073/pnas.97.8.4023</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC18135">18135</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10760274">10760274</a>.</li> <li>Mu J, Brozinick JT, Valladares O, Bucan M, Birnbaum MJ (2001). <a href="https://doi.org/10.1016%2FS1097-2765%2801%2900251-9">"A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle"</a>. <i>Mol. Cell</i>. 7 (5): 1085–94. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS1097-2765%2801%2900251-9">10.1016/S1097-2765(01)00251-9</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11389854">11389854</a>.</li> <li>Minokoshi Y, Kim YB, Peroni OD, Fryer LG, Müller C, Carling D, Kahn BB (2002). "Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase". <i>Nature</i>. 415 (6869): 339–43. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2002Natur.415..339M">2002Natur.415..339M</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F415339a">10.1038/415339a</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11797013">11797013</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4409274">4409274</a>.</li> <li>Dubbelhuis PF, Meijer AJ (2002). "Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase". <i>FEBS Lett</i>. 521 (1–3): 39–42. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0014-5793%2802%2902815-6">10.1016/S0014-5793(02)02815-6</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12067722">12067722</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:32171292">32171292</a>.</li> <li>Esumi H, Izuishi K, Kato K, Hashimoto K, Kurashima Y, Kishimoto A, Ogura T, Ozawa T (2002). <a href="https://doi.org/10.1074%2Fjbc.M112270200">"Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner"</a>. <i>J. Biol. Chem</i>. 277 (36): 32791–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M112270200">10.1074/jbc.M112270200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12091379">12091379</a>.</li> <li>Nielsen JN, Mustard KJ, Graham DA, Yu H, MacDonald CS, Pilegaard H, Goodyear LJ, Hardie DG, Richter EA, Wojtaszewski JF (2003). "5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle". <i>J. Appl. Physiol</i>. 94 (2): 631–41. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1152%2Fjapplphysiol.00642.2002">10.1152/japplphysiol.00642.2002</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12391032">12391032</a>.</li> <li>Wojtaszewski JF, Mourtzakis M, Hillig T, Saltin B, Pilegaard H (2002). "Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise". <i>Biochem. Biophys. Res. Commun</i>. 298 (3): 309–16. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0006-291X%2802%2902465-8">10.1016/S0006-291X(02)02465-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12413941">12413941</a>.</li> <li>Hallows KR, McCane JE, Kemp BE, Witters LA, Foskett JK (2003). <a href="https://doi.org/10.1074%2Fjbc.M210621200">"Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells"</a>. <i>J. Biol. Chem</i>. 278 (2): 998–1004. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M210621200">10.1074/jbc.M210621200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12427743">12427743</a>.</li> <li>Zong H, Ren JM, Young LH, Pypaert M, Mu J, Birnbaum MJ, Shulman GI (2003). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC138551">"AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 99 (25): 15983–7. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.252625599">10.1073/pnas.252625599</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC138551">138551</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12444247">12444247</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Aguan K, Scott J, See CG, Sarkar NH (Dec 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. doi:10.1016/0378-1119(94)90174-0. PMID 7959015. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>"Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> </ol>