A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins

@article{Rouse1994ANK,
  title={A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins},
  author={John Rouse and Philip Cohen and Sylviane Trigon and Michel Morange and Ana Alonso-Llamazares and Daniel Zamanillo and Timothy Hunt and Angel R. Nebreda},
  journal={Cell},
  year={1994},
  volume={78},
  pages={1027-1037}
}
Constitutive Activation of Mitogen-activated Protein Kinase-activated Protein Kinase 2 by Mutation of Phosphorylation Sites and an A-helix Motif (*)
TLDR
A dual mechanism of MAPKAP kinase 2 activation is suggested by phosphorylation of Thr-205 inside the catalytic domain and byosphorylated Thr-317 outside the catalysttic domain involving an autoinhibitory A-helix motif.
Stimulation of the stress-activated mitogen-activated protein kinase subfamilies in perfused heart. p38/RK mitogen-activated protein kinases and c-Jun N-terminal kinases are activated by ischemia/reperfusion.
TLDR
Using the isolated perfused rat heart, it is shown that global ischemia does not activate the 42- and 44-kD extracellular signal-regulated (protein) kinase (ERK) subfamily of MAPKs but rather stimulates a 38- kD activator ofMAPK-activated protein kinase-2 (MAPKAPK2) which is maintained during reperfusion.
The Stress Inducer Arsenite Activates Mitogen-activated Protein Kinases Extracellular Signal-regulated Kinases 1 and 2 via a MAPK Kinase 6/p38-dependent Pathway*
TLDR
It is shown here that the stress cascade activator arsenite activates extracellular signal-regulated kinase (ERK) in addition to p38 albeit with different kinetics, providing the first evidence for a p38 dependent activation of the mitogenic kinase cascade in stress-stimulated cells.
Cellular stresses and cytokines activate multiple mitogen-activated-protein kinase kinase homologues in PC12 and KB cells.
TLDR
The results demonstrate unexpected complexity in the upstream regulation of stress and cytokine-stimulated kinase cascades and indicate that the selection of the appropriate SAPKK varies with both the stimulus and the cell type.
Activation of Protein Kinase Cascades by Osmotic Shock (*)
TLDR
The results suggest that the MAPK cascade consisting of Raf-1, MAPKK, and MAPK and the SAPK cascade consists of MEKK, XMEK2, and SAPK are both activated in response to osmotic shock.
Pro-inflammatory Cytokines and Environmental Stress Cause p38 Mitogen-activated Protein Kinase Activation by Dual Phosphorylation on Tyrosine and Threonine (*)
TLDR
It is demonstrated that p38, like JNK, is activated by treatment of cells with pro-inflammatory cytokines and environmental stress and the mechanism of p38 activation is mediated by dual phosphorylation on Thr-180 and Tyr-182.
Both Binding and Activation of p38 Mitogen-Activated Protein Kinase (MAPK) Play Essential Roles in Regulation of the Nucleocytoplasmic Distribution of MAPK-Activated Protein Kinase 5 by Cellular Stress
TLDR
Enhanced green fluorescent protein fusion proteins are used to analyze the subcellular localization of MAPK-activated protein kinase 5 and it is shown that stress-induced activation of the p38 MAPK stimulates the chromosomal region maintenance 1 protein-dependent nuclear export of MK5.
Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27.
TLDR
The results provide strong support to the idea that activation of p38 during adverse environmental conditions serves a homeostatic function aimed at regulating actin dynamics that would otherwise be destabilized during stress.
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References

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The stress-activated protein kinase subfamily of c-Jun kinases
TLDR
The kinase p54s are the principal c-Jun N-terminal kinases activated by cellular stress and tumour necrosis factor (TNF)-α, hence they are designated stress-activated protein kinases, or SAPKs.
Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2.
TLDR
Mitogen-activated protein-kinase (MAP) kinase-activatedprotein kinases 1 and 2, were found to phosphorylate bacterially expressed human tyrosine hydroxylase in vitro at comparable rates to other proteins thought to be physiological substrates of these protein kinases.
MAPKAP kinase‐2; a novel protein kinase activated by mitogen‐activated protein kinase.
TLDR
Results indicate that MAP kinase activates at least two distinct protein kinases, suggesting that it represents a point at which the growth factor‐stimulated protein kinase cascade bifurcates.
Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
TLDR
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.
Dissection of the protein kinase cascade by which nerve growth factor activates MAP kinases
TLDR
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.
Stress‐ and mitogen‐induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance.
TLDR
The results suggest that chaperone properties of the small heat shock proteins contribute to the increased cellular thermoresistance in a phosphorylation‐independent manner.
Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor.
TLDR
The results suggest that sustained activation of theMAP kinase cascade may be required for MAP kinase to enter the nucleus, where it may initiate the gene transcription events required for neuronal differentiation of PC12 cells.
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