Serine/Threonine-Protein Phosphatase 2A
Since Krebs and Fischer (1956) discovered that the activity of an enzyme (glycogen phosphorylase) can be regulated by a reversible phosphorylation, much attention has been paid to the enzymes catalyzing these covalent modifications: the protein kinases and protein phosphatases. As opposed to protein kinases, it has taken much more time to understand the action of protein phosphatases, mainly because of their complex molecular structure and broad substrate specificities. Nevertheless, protein phosphatases are equally important in controlling biochemical pathways, adding reversibility and sensitivity to these processes.
While the first kinase (phosphorylase kinase) was isolated soon after the discovery of the concept of reversible protein phosphorylation, the biochemical isolation of the first phosphataseneeded about 20 more years: ethanol denaturation (accidently...
- Dodge-Kafka KL, Bauman A, Mayer N, Henson E, Heredia L, Ahn J, et al. cAMP-stimulated protein phosphatase 2A activity associated with muscle A kinase-anchoring protein (mAKAP) signaling complexes inhibits the phosphorylation and activity of the cAMP-specific phosphodiesterase PDE4D3. J Biol Chem. 2010;285:11078–86. doi:10.1074/jbc.M109.034868.CrossRefPubMedPubMedCentralGoogle Scholar
- Haesen D, Sents W, Ivanova E, Lambrecht C, Janssens V. Cellular inhibitors of protein phosphatase PP2A in cancer. Biomed Res India. 2012;23:197–211.Google Scholar