title: Expression and characterization of MAP kinases in bacteria.
abstract: Mitogen-activated protein kinases (MAPKs) are common signal transducers in all eukaryotic organisms. MAPKs are activated by protein kinase cascades consisting of MAPK kinases (MAP2Ks) and MAPK kinase kinases (MAP3Ks). Extracellular-signal regulated kinases 1 and 2 (ERK1/2) are the best characterized MAPKs. Like other MAPKs their activity is regulated by dual phosphorylation as well as dephosphorylation by a host of phosphoprotein phosphatases. The ability to phosphorylate or thiophosphorylate ERK2 in vitro, as described here, is valuable for use in downstream applications designed to investigate MAPK signaling networks.
authors.affiliation: Department of Pharmacology, The University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park Road, Dallas, TX 75390-9041, USA.
authors.forename: Charles J
authors.initials: CJ
authors.lastname: Heise
authors.forename: Melanie H
authors.initials: MH
authors.lastname: Cobb
mesh_terms: D001419:Bacteria / Q000201:enzymology / Q000378:metabolism*; D004789:Enzyme Activation; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D048369:MAP Kinase Kinase 1 / Q000235:genetics / Q000378:metabolism; D020935:MAP Kinase Signaling System; D019950:Mitogen-Activated Protein Kinase 1 / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008967:Molecular Biology / Q000379:methods*; D009154:Mutation; D010766:Phosphorylation
chemical_list: D019950:Mitogen-Activated Protein Kinase 1; D048369:MAP Kinase Kinase 1