(Q28142838)

English

Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway

scientific article (publication date: 7 May 1999)

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Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway (English)

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author name string

J L Todd

1

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K G Tanner

2

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J M Denu

3

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language of work or name

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publication date

7 May 1999

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Journal of Biological Chemistry

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274

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19

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13271-80

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Form and function in protein dephosphorylation

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A Tyr/Ser protein phosphatase encoded by vaccinia virus

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Protein phosphatases and the regulation of MAP kinase activity

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Mitogen-activated protein kinase pathways

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Signal transduction by the c-Jun N-terminal kinase (JNK)--from inflammation to development

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Transcriptional regulation by extracellular signals: mechanisms and specificity

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MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo

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Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1

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Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines

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The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation

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Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase

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PAC-1: a Mitogen-Induced Nuclear Protein Tyrosine Phosphatase

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A novel cytoplasmic dual specificity protein tyrosine phosphatase implicated in muscle and neuronal differentiation

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MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase

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Repression of mitogen-activated protein kinases ERK1/ERK2 activity by a protein tyrosine phosphatase in rat fibroblasts transformed by upstream oncoproteins

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Regulation of p42 mitogen-activated-protein kinase activity by protein phosphatase 2A under conditions of growth inhibition by epidermal growth factor in A431 cells

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Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines.

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Rapid deactivation of MAP kinase in PC12 cells occurs independently of induction of phosphatase MKP-1.

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Insulin and tumor-promoting agent regulate an inhibitor of the 44-kDa mitogen-activated protein kinase/extracellular signal-regulated protein kinase 1 in fibroblasts

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EGF-mediated phosphorylation of extracellular signal-regulated kinases in osteoblastic cells

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Induction of mitogen-activated protein kinase phosphatase 1 by the stress-activated protein kinase signaling pathway but not by extracellular signal-regulated kinase in fibroblasts

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An emerging family of dual specificity MAP kinase phosphatases

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Expression cloning of a human dual-specificity phosphatase

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The purification and characterization of a human dual-specific protein tyrosine phosphatase

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A catalytic mechanism for the dual-specific phosphatases

1 reference

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Crystal structure of the dual specificity protein phosphatase VHR

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Redox modulation of tyrosine phosphorylation-dependent signal transduction pathways

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Redox regulation of NF-kappa B activation

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Oxidants as stimulators of signal transduction

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Requirement for generation of H2O2 for platelet-derived growth factor signal transduction

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Activation of mitogen-activated protein kinase by H2O2. Role in cell survival following oxidant injury

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The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways

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Interdependent domains controlling the enzymatic activity of mitogen-activated protein kinase kinase 1.

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Role of the stress-activated/c-Jun NH2-terminal protein kinase pathway in the cellular response to adriamycin and other chemotherapeutic drugs

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Reconstitution of mitogen-activated protein kinase phosphorylation cascades in bacteria. Efficient synthesis of active protein kinases

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Purification and kinetic characterization of the mitogen-activated protein kinase phosphatase rVH6.

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Anisomycin selectively desensitizes signalling components involved in stress kinase activation and fos and jun induction

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A good antisense molecule is hard to find

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Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases

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Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions

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Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase

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Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin

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Rapid activation and nuclear translocation of mitogen-activated protein kinases in response to physiological concentration of glucose in the MIN6 pancreatic beta cell line.

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Activation and nuclear translocation of mitogen-activated protein kinases by polyomavirus middle-T or serum depend on phosphatidylinositol 3-kinase.

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Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation

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Protein phosphatase 2A positively and negatively regulates Ras1-mediated photoreceptor development in Drosophila.

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Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast.

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The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity

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Effects of H2O2 on protein tyrosine phosphatase activity in HER14 cells

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Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor

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Signalling and superinduction

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10.1074/JBC.274.19.13271

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