PRKAB1

From Wikipedia, the free encyclopedia

Protein kinase, AMP-activated, beta 1 non-catalytic subunit

PDB rendering based on 1z0m.

Available structures: 1z0m, 1z0n

Identifiers

Symbol(s)

PRKAB1; AMPK; HAMPKb; MGC17785

External IDs

OMIM: 602740 MGI: 1336167 HomoloGene: 38160

Gene ontology
Molecular Function:	• hydrolase activity, hydrolyzing O-glycosyl compounds
Cellular Component:	• nucleus
Biological Process:	• carbohydrate metabolic process • fatty acid biosynthetic process • signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006253 (mRNA)
NP_006244 (protein)

NM_031869 (mRNA)
NP_114075 (protein)

Location

Chr 12: 118.59 - 118.6 Mb

Chr 5: 116.27 - 116.29 Mb

Pubmed search

[1]

[2]

Protein kinase, AMP-activated, beta 1 non-catalytic subunit, also known as PRKAB1, is a human gene.^[1]

The protein encoded by this gene is a regulatory 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. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.^[1]

[edit] References

^ ^a ^b Entrez Gene: PRKAB1 protein kinase, AMP-activated, beta 1 non-catalytic subunit.

[edit] Further reading

Carling D (2004). "The AMP-activated protein kinase cascade--a unifying system for energy control.". Trends Biochem. Sci. 29 (1): 18–24. PMID 14729328.
Stapleton D, Mitchelhill KI, Gao G, et al. (1996). "Mammalian AMP-activated protein kinase subfamily.". J. Biol. Chem. 271 (2): 611–4. PMID 8557660.
Gao G, Fernandez CS, Stapleton D, et al. (1996). "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase.". J. Biol. Chem. 271 (15): 8675–81. PMID 8621499.
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.
Dyck JR, Gao G, Widmer J, et al. (1996). "Regulation of 5'-AMP-activated protein kinase activity by the noncatalytic beta and gamma subunits.". J. Biol. Chem. 271 (30): 17798–803. PMID 8663446.
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.
Mitchelhill KI, Michell BJ, House CM, et al. (1997). "Posttranslational modifications of the 5'-AMP-activated protein kinase beta1 subunit.". J. Biol. Chem. 272 (39): 24475–9. PMID 9305909.
Thornton C, Snowden MA, Carling D (1998). "Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle.". J. Biol. Chem. 273 (20): 12443–50. PMID 9575201.
Cheung PC, Salt IP, Davies SP, et al. (2000). "Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding.". Biochem. J. 346 Pt 3: 659–69. PMID 10698692.
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.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Lemieux K, Konrad D, Klip A, Marette A (2003). "The AMP-activated protein kinase activator AICAR does not induce GLUT4 translocation to transverse tubules but stimulates glucose uptake and p38 mitogen-activated protein kinases alpha and beta in skeletal muscle.". FASEB J. 17 (12): 1658–65. doi:10.1096/fj.02-1125com. PMID 12958172.
Landree LE, Hanlon AL, Strong DW, et al. (2004). "C75, a fatty acid synthase inhibitor, modulates AMP-activated protein kinase to alter neuronal energy metabolism.". J. Biol. Chem. 279 (5): 3817–27. doi:10.1074/jbc.M310991200. PMID 14615481.
Inoki K, Zhu T, Guan KL (2004). "TSC2 mediates cellular energy response to control cell growth and survival.". Cell 115 (5): 577–90. PMID 14651849.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Andersson U, Filipsson K, Abbott CR, et al. (2004). "AMP-activated protein kinase plays a role in the control of food intake.". J. Biol. Chem. 279 (13): 12005–8. doi:10.1074/jbc.C300557200. PMID 14742438.
Pilon G, Dallaire P, Marette A (2004). "Inhibition of inducible nitric-oxide synthase by activators of AMP-activated protein kinase: a new mechanism of action of insulin-sensitizing drugs.". J. Biol. Chem. 279 (20): 20767–74. doi:10.1074/jbc.M401390200. PMID 14985344.
Shaw RJ, Kosmatka M, Bardeesy N, et al. (2004). "The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress.". Proc. Natl. Acad. Sci. U.S.A. 101 (10): 3329–35. doi:10.1073/pnas.0308061100. PMID 14985505.
Kim EK, Miller I, Aja S, et al. (2004). "C75, a fatty acid synthase inhibitor, reduces food intake via hypothalamic AMP-activated protein kinase.". J. Biol. Chem. 279 (19): 19970–6. doi:10.1074/jbc.M402165200. PMID 15028725.