Recombinant Mouse 5-AMP-activated protein kinase subunit beta-1 (Prkab1)

Function

Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3) (By similarity)

Subunit

AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By similarity)

• Valentijn L.J. et al. 5'-AMP-activated protein kinase subunit beta interacts with the p42 subunit of translation initiation factor eIF3. (NOV-)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Trost M. et al. The phagosomal proteome in interferon-gamma-activated macrophages. — Immunity (2009)
• Sweet S.M. et al. Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry. — Mol. Cell. Proteomics (2009)
• Huttlin E.L. et al. A tissue-specific atlas of mouse protein phosphorylation and expression. — Cell (2010)
• Loffler A.S. et al. Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop. — Autophagy (2011)
• Park J. et al. SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways. — Mol. Cell (2013)
• Cattin M.E. et al. Deletion of MLIP (muscle-enriched A-type lamin-interacting protein) leads to cardiac hyperactivation of Akt/mammalian target of rapamycin (mTOR) and impaired cardiac adaptation. — J. Biol. Chem. (2015)