Heterogeneous expression of four MAP kinase isoforms in human tissues

  title={Heterogeneous expression of four MAP kinase isoforms in human tissues},
  author={Fernando A. González and David L Raden and Mark R. Rigby and Roger J. Davis},
  journal={FEBS Letters},
Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
Recent progress towards understanding AP-1 regulation by the ERK, JNK, and p38 MAP kinase signal transduction pathways is reviewed.
Phosphorylation of MAP Kinases by MAP/ERK Involves Multiple Regions of MAP Kinases*
Experimental results and modeling support the conclusion that the specificity of MEK/MAP kinase phosphorylation results from multiple contacts, including surfaces in both the N- and C-terminal domains.
Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions.
Nonenzymatic mechanisms that impact MAP kinase functions and findings from gene disruption studies are highlighted and particular emphasis is on ERK1/2.
The Mouse p44 Mitogen-activated Protein Kinase (Extracellular Signal-regulated Kinase 1) Gene
A complex pattern of transcriptional regulation of the mouse p44 MAPK promoter is revealed, being comparable with the activity of the Rous sarcoma virus promoter.
MAP kinase pathways.
  • M. Cobb
  • Biology
    Progress in biophysics and molecular biology
  • 1999
Regulation and Structure of the MAP Kinases ERK1 and ERK2
X-ray crystallographic studies of ERK2 have revealed important features of its phosphoregulatory mechanism and should be valuable in developing specific MAP kinase inhibitors.


Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
It is demonstrated that MAP kinase is only active when both tyrosyl and threonyl residues are phosphorylated and suggested therefore that the enzyme functions in vivo to integrate signals from two distinct transduction pathways.
An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control.
A protein kinase characterized by its ability to phosphorylate microtubule-associated protein-2 (MAP2), is thought to be an early intermediate in an insulin-stimulated phosphorylation cascade and in
Dissection of the protein kinase cascade by which nerve growth factor activates MAP kinases
The 'MAP kinase kinases' (MAPKKs) in PC12 cells which are activated by NGF are identified and it is reported that MAPKKs are dependent on serine/threonine phosphorylated for activity and promote phosphorylation of serine-threonines and tyrosine residues on MAPKs.
Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation
Interestingly, the region in p42P which contains the regulatory phosphorylations is perfectly conserved in all four kinases, raising the possibility that both the function and the mechanisms of regulation have been evolutionarily conserving in this kinase family.
Phosphorylation of c-jun mediated by MAP kinases
Evidence is presented that mitogen-activated protein-serine (MAP) kinases (pp54 and pp42/44) specifically phosphorylate these sites and that their phosphorylation positively regulates the transacting activity of c-jun.
Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine.
Bacterial expression of mouse gene Erk-1 yielded an active kinase with the same substrate specificity shown for ERK1 protein purified from rat cells, and autophosphorylated on tyrosine in addition to serine and threonine residues, predicting that autoph phosphorylation may play an important role in ErK-1/ERK1 regulation.
Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
These studies suggest that a step in insulin signalling involves sequential activation by phosphorylation of at least two serine/threonine protein kinases.
Multiple components in an epidermal growth factor-stimulated protein kinase cascade. In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase.
It is proposed that the in vitro activation involves protein phosphorylation, stimulated by the action of novel MBP kinase activating factors that represent intermediate components in a growth factor-stimulated kinase cascade.