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PRKAA1

Introduction

Protein kinase, AMP-activated, alpha 1 catalytic subunit, also known as PRKAA1, is a human gene.[1]

The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5′-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed.[1]

References

References

  1. ↑ 1.0 1.1 “Entrez Gene: PRKAA1 protein kinase, AMP-activated, alpha 1 catalytic subunit”.
Further reading

Further reading

  • Munday MR, Campbell DG, Carling D, Hardie DG (1988). “Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase”. Eur. J. Biochem. 175 (2): 331–8. PMID 2900138.
  • Stapleton D, Mitchelhill KI, Gao G; et al. (1996). “Mammalian AMP-activated protein kinase subfamily”. J. Biol. Chem. 271 (2): 611–4. PMID 8557660.
  • Woods A, Cheung PC, Smith FC; et al. (1996). “Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro”. J. Biol. Chem. 271 (17): 10282–90. PMID 8626596.
  • Hawley SA, Davison M, Woods A; et al. (1996). “Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase”. J. Biol. Chem. 271 (44): 27879–87. PMID 8910387.
  • 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.
  • Velasco G, Gómez del Pulgar T, Carling D, Guzmán M (1998). “Evidence that the AMP-activated protein kinase stimulates rat liver carnitine palmitoyltransferase I by phosphorylating cytoskeletal components”. FEBS Lett. 439 (3): 317–20. PMID 9845345.
  • Crute BE, Seefeld K, Gamble J; et al. (1999). “Functional domains of the alpha1 catalytic subunit of the AMP-activated protein kinase”. J. Biol. Chem. 273 (52): 35347–54. PMID 9857077.
  • 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.
  • Hallows KR, Raghuram V, Kemp BE; et al. (2000). “Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase”. J. Clin. Invest. 105 (12): 1711–21. PMID 10862786.
  • Zhang QH, Ye M, Wu XY; et al. (2001). “Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells”. Genome Res. 10 (10): 1546–60. PMID 11042152.
  • Chen ZP, McConell GK, Michell BJ; et al. (2000). “AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation”. Am. J. Physiol. Endocrinol. Metab. 279 (5): E1202–6. PMID 11052978.
  • Blázquez C, Geelen MJ, Velasco G, Guzmán M (2001). “The AMP-activated protein kinase prevents ceramide synthesis de novo and apoptosis in astrocytes”. FEBS Lett. 489 (2–3): 149–53. PMID 11165240.
  • Diggle TA, Subkhankulova T, Lilley KS; et al. (2001). “Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity”. Biochem. J. 353 (Pt 3): 621–6. PMID 11171059.
  • Wang X, Li W, Williams M; et al. (2001). “Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase”. EMBO J. 20 (16): 4370–9. doi:10.1093/emboj/20.16.4370. PMID 11500364.
  • Xi X, Han J, Zhang JZ (2001). “Stimulation of glucose transport by AMP-activated protein kinase via activation of p38 mitogen-activated protein kinase”. J. Biol. Chem. 276 (44): 41029–34. doi:10.1074/jbc.M102824200. PMID 11546797.
  • Fryer LG, Foufelle F, Barnes K; et al. (2002). “Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells”. Biochem. J. 363 (Pt 1): 167–74. PMID 11903059.
  • Yang CS, Weiner H (2002). “Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol”. Arch. Biochem. Biophys. 400 (1): 105–10. doi:10.1006/abbi.2002.2778. PMID 11913976.
  • Bolster DR, Crozier SJ, Kimball SR, Jefferson LS (2002). “AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling”. J. Biol. Chem. 277 (27): 23977–80. doi:10.1074/jbc.C200171200. PMID 11997383.
  • 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.
  • Horman S, Browne G, Krause U; et al. (2003). “Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis”. Curr. Biol. 12 (16): 1419–23. PMID 12194824.

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