Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase

@article{Saxena1999CrosstalkBC,
  title={Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase},
  author={Manju Saxena and Scott M. Williams and Kjetil Task{\'e}n and Tomas Mustelin},
  journal={Nature Cell Biology},
  year={1999},
  volume={1},
  pages={305-310}
}
The haematopoietic protein tyrosine phosphatase (HePTP) is a negative regulator of the MAP kinases Erk1, Erk2 and p38. HePTP binds to these kinases through a kinase-interaction motif (KIM) in its non-catalytic amino terminus and inactivates them by dephosphorylating the critical phosphorylated tyrosine residue in their activation loop. Here we show that cyclic-AMP-dependent protein kinase (PKA) phosphorylates serine residue 23 in the KIM of HePTP in vitro and in intact cells. This modification… 
Haematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T-cells: dynamics and subcellular location.
TLDR
HePTP is under continuous control by PKA and a serine-specific phosphatase, probably PP1, in T-cells and this basal phosphorylation at Ser-23 can rapidly change in response to external stimuli, which will affect the ability of HePTP to inhibit the ERK and p38 MAP kinases.
A Novel Regulatory Mechanism of Map Kinases Activation and Nuclear Translocation Mediated by Pka and the Ptp-Sl Tyrosine Phosphatase
TLDR
Findings support the existence of a novel mechanism by which PKA may regulate the activation and translocation to the nucleus of MAP kinases.
Enzymatic Activity and Substrate Specificity of Mitogen-activated Protein Kinase p38α in Different Phosphorylation States*
TLDR
The quantitative contributions of phosphorylation of Thr, Tyr, or both to the activation of p38α and to the substrate specificity for various phosphatases are revealed.
Phosphotyrosine-specific Phosphatase PTP-SL Regulates the ERK5 Signaling Pathway*
TLDR
Findings indicate a direct regulatory influence of PTP-SL on the ERK5 pathway and corresponding downstream responses of the cell, which is critical for the definition of a specific cellular response.
Catalytic activation of mitogen-activated protein (MAP) kinase phosphatase-1 by binding to p38 MAP kinase: critical role of the p38 C-terminal domain in its negative regulation.
TLDR
These studies provide the first example of catalytic activation of a nuclear MAP kinase phosphatase through direct binding to aMAP kinase, suggesting that such a regulatory mechanism may play an important role in the feedback control of MAP kinases signalling in the nuclear compartment.
Discordance between the Binding Affinity of Mitogen-activated Protein Kinase Subfamily Members for MAP Kinase Phosphatase-2 and Their Ability to Activate the Phosphatase Catalytically*
TLDR
This report found that the catalytic activity of MKP-2 was enhanced dramatically by ERK and JNK but was affected only minimally by p38, and provided a mechanistic explanation for the substrate preference of MKp-2 and suggest that catalytic activation of MKF2 upon binding to its substrates is crucial for its function.
Tyrosine-specific MAPK phosphatases and the control of ERK signaling in PC12 cells
TLDR
The finding that robust changes in tyrosine-specific MAPK phosphatase expression levels have minor effects on temporal ERK1/2 activity control in PC12 cells suggests that dual-specificity MAPKosphatases may act as major regulators of growth factor-induced ERK 1/2 signaling in these cells.
ERK2 Shows a Restrictive and Locally Selective Mechanism of Recognition by Its Tyrosine Phosphatase Inactivators Not Shared by Its Activator MEK1*
TLDR
The results provide evidence that the ERK2 docking groove is more restrictive and selective for its tyrosine phosphatase inactivators than for MEK1/2 and indicate that distinct ERK 2 residues modulate the docking interactions with activating and inactivating effectors.
Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents.
TLDR
It is suggested that intracellular redox conditions could modulate the activity and subcellular location of ERK1/2 and p38alpha by controlling their association with their regulatory PTPs.
Molecular Determinants of Substrate Recognition in Hematopoietic Protein-tyrosine Phosphatase*
TLDR
The results suggest that substrate specificity is conferred upon HePTP by both negative and positive selections, and that ERK2 dephosphorylation is achieved by a bipartite protein-protein interaction mechanism.
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