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… 
View on Nature
ncbi.nlm.nih.gov
202 Citations
Highly Influential Citations
7
Background Citations
46
Methods Citations
2
Results Citations
1

202 Citations

Citation Type

Citation Type

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.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 57 REFERENCES
Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase.
TLDR
Another homologous but nonselective phosphatase, MKP-4, bound and was activated by ERK2, JNK/SAPK, and p38 MAP kinases and was resistant to enzymatic inactivation by MKP.
Inhibition of T Cell Signaling by Mitogen-activated Protein Kinase-targeted Hematopoietic Tyrosine Phosphatase (HePTP)*
TLDR
It is proposed that HePTP plays a negative role in antigen receptor signaling by specifically regulating MAP kinases in the cytosol and at early time points of T cell activation before the activation-induced expression of nuclear dual-specific MAP kinase phosphatases.
MKP-3, a Novel Cytosolic Protein-tyrosine Phosphatase That Exemplifies a New Class of Mitogen-activated Protein Kinase Phosphatase (*)
TLDR
Observations indicate that MKP-3 is a novel dual-specificity phosphatase that displays a distinct tissue distribution, subcellular localization, and regulated expression, suggesting a unique function in controlling MAP kinase family members.
Regulation of the Lck SH2 Domain by Tyrosine Phosphorylation*
TLDR
It is reported that phosphorylation at Tyr192 reduced the capacity of the isolated SH2 domain to bind a high affinity peptide ligand and Tyr(P)-containing cellular proteins, and represented a novel mechanism for the regulation of the function of SH2 domains.
PTP‐PEST: a protein tyrosine phosphatase regulated by serine phosphorylation.
TLDR
The results suggest that both PKC and PKA are capable of phosphorylating, and therefore inhibiting, PTP‐PEST in vivo, offering a mechanism whereby signal transduction pathways acting through either PKA or PKC may directly influence cellular processes involving reversible tyrosine phosphorylation.
Inhibition by cAMP of Ras-dependent activation of Raf.
TLDR
CAMP appears to inhibit signal transmission from Ras by preventing Ras-dependent activation of Raf-1 and ERK kinases, which are key events in mitogenic signalling.
Negative Regulation of T Cell Antigen Receptor Signal Transduction by Hematopoietic Tyrosine Phosphatase (HePTP)*
TLDR
It is suggested that HePTP plays an active negative role in TCR signaling by dephosphorylating one or several signaling molecules between the receptor and the mitogen-activated protein kinase pathway.
The human p50csk tyrosine kinase phosphorylates p56lck at Tyr‐505 and down regulates its catalytic activity.
TLDR
A human cytosolic 50 kDa protein tyrosine kinase is characterized, p50csk, which specifically phosphorylates Tyr‐505 of p56lck and a synthetic peptide containing this site, which is suggested to negatively regulates p56 lck and perhaps other cellular src family kinases.
Involvement of Phosphatidylinositol 3-Kinase in NFAT Activation in T Cells*
TLDR
The results suggest that PI3-K is involved in NFAT activation through a complex adaptor function of its regulatory subunit and that its lipid kinase activity is dispensable for this effect.
MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
...
1
2
3
4
5
...