The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases (Q44039955)

29 November 2017

title

The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases (English)

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29 November 2017

Bo Zhou

1

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29 November 2017

Zhi-Xin Wang

2

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29 November 2017

Yu Zhao

3

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29 November 2017

David L Brautigan

4

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29 November 2017

Zhong-Yin Zhang

5

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29 November 2017

language of work or name

English

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publication date

24 June 2002

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Journal of Biological Chemistry

29 November 2017

published in

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29 November 2017

volume

277

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29 November 2017

issue

35

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29 November 2017

page(s)

31818-31825

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https://api.crossref.org/works/10.1074%2FJBC.M203969200

29 November 2017

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Colworth Medal Lecture. Structural studies of reversible protein phosphorylation and protein phosphatases

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The activity of the extracellular signal-regulated kinase 2 is regulated by differential phosphorylation in the activation loop

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The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3.

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PTP-ER, a novel tyrosine phosphatase, functions downstream of Ras1 to downregulate MAP kinase during Drosophila eye development

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Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase

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1 reference

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PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.

21 January 2018

1 reference

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Negative regulation of T cell antigen receptor signal transduction by hematopoietic tyrosine phosphatase (HePTP)

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Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)

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1 reference

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Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm

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1 reference

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Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development

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The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation.

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Simian virus 40 small t antigen cooperates with mitogen-activated kinases to stimulate AP-1 activity

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A two-component system that regulates an osmosensing MAP kinase cascade in yeast

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Protein phosphatase 2C, encoded by ptc1+, is important in the heat shock response of Schizosaccharomyces pombe

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Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways

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Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1

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1 reference

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Tyrosine-phosphorylated extracellular signal--regulated kinase associates with the Golgi complex during G2/M phase of the cell cycle: evidence for regulation of Golgi structure

21 January 2018

1 reference

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Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II.

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Structural basis of plasticity in protein tyrosine phosphatase 1B substrate recognition

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Substrate specificities of catalytic fragments of protein tyrosine phosphatases (HPTP beta, LAR, and CD45) toward phosphotyrosylpeptide substrates and thiophosphotyrosylated peptides as inhibitors

21 January 2018

1 reference

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Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation

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21 January 2018

Identifiers

DOI

10.1074/JBC.M203969200

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29 November 2017

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