PRKAA1

From Wikipedia, the free encyclopedia

Protein kinase, AMP-activated, alpha 1 catalytic subunit

PDB rendering based on 2h6d.

Available structures: 2h6d

Identifiers

Symbol(s)

PRKAA1; AMPK; AMPKa1; MGC33776; MGC57364

External IDs

OMIM: 602739 MGI: 2145955 HomoloGene: 49590

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • cAMP-dependent protein kinase activity • ATP binding • transferase activity • eukaryotic elongation factor-2 kinase activator activity
Cellular Component:	• intracellular
Biological Process:	• activation of MAPK activity • response to hypoxia • protein amino acid phosphorylation • fatty acid biosynthetic process • cholesterol biosynthetic process • signal transduction • negative regulation of protein biosynthetic process • positive regulation of cholesterol biosynthetic process • positive regulation of gluconeogenesis • positive regulation of anti-apoptosis • negative regulation of glucosylceramide biosynthetic process • positive regulation of fatty acid oxidation • positive regulation of glucose import

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006251 (mRNA)
NP_006242 (protein)

XM_973840 (mRNA)
XP_978934 (protein)

Location

Chr 5: 40.8 - 40.83 Mb

Chr 15: 5.09 - 5.13 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: PRKAA1 protein kinase, AMP-activated, alpha 1 catalytic subunit.

[edit] 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.