PRKAB1 explained

5'-AMP-activated protein kinase subunit beta-1 is an enzyme that in humans is encoded by the PRKAB1 gene.[1] [2]

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.[2]

Interactions

PRKAB1 has been shown to interact with PRKAG2[3] and PRKAG1.[3]

The 5'-AMP-activated protein kinase beta subunit interaction domain (AMPKBI) is a conserved domain found in the beta subunit of the 5-AMP-activated protein kinase complex, and its yeast homologues Sip1 (SNF1-interacting protein 1), Sip2 (SNF1-interacting protein 2) and Gal83 (galactose metabolism 83), which are found in the SNF1 (sucrose non-fermenting) kinase complex.[4] This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known.[5]

Symbol:AMPKBI
AMPKBI
Pfam:PF04739
Interpro:IPR006828

Further reading

External links

Notes and References

  1. Stapleton D, Mitchelhill KI, Gao G, Widmer J, Michell BJ, Teh T, House CM, Fernandez CS, Cox T, Witters LA, Kemp BE . Mammalian AMP-activated protein kinase subfamily . J Biol Chem . 271 . 2 . 611–4 . February 1996 . 8557660 . 10.1074/jbc.271.2.611 . free .
  2. Web site: Entrez Gene: PRKAB1 protein kinase, AMP-activated, beta 1 non-catalytic subunit.
  3. Cheung . P C . Salt I P . Davies S P . Hardie D G . Carling D . March 2000 . Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding . Biochem. J. . 346 . 3. 659–69 . 0264-6021. 10698692 . 1220898 . 10.1042/0264-6021:3460659.
  4. Gao G, Fernandez CS, Stapleton D, Auster AS, Widmer J, Dyck JR, Kemp BE, Witters LA . Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase . J. Biol. Chem. . 271 . 15 . 8675–81 . April 1996 . 8621499 . 10.1074/jbc.271.15.8675. free .
  5. Yang X, Jiang R, Carlson M . A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex . EMBO J. . 13 . 24 . 5878–86 . December 1994 . 7813428 . 395563 . 10.1002/j.1460-2075.1994.tb06933.x.