Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites (Q28609103)

3 February 2017

title

Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites (English)

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3 February 2017

Stéphane Ory

1

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3 February 2017

Ming Zhou

2

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3 February 2017

Thomas P. Conrads

3

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3 February 2017

Timothy D. Veenstra

4

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3 February 2017

Deborah K. Morrison

5

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3 February 2017

language of work or name

English

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publication date

19 August 2003

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3 February 2017

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3 February 2017

volume

13

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3 February 2017

issue

16

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3 February 2017

page(s)

1356–1364

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The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans

3 February 2017

cites work

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The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction

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KSR, a novel protein kinase required for RAS signal transduction

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C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold, KSR1

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KSR is a scaffold required for activation of the ERK/MAPK module

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Critical contribution of linker proteins to Raf kinase activation

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C. elegans ksr-1 and ksr-2 have both unique and redundant functions and are required for MPK-1 ERK phosphorylation

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Scaffolding and protein interactions in MAP kinase modules.

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Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction

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Identification of constitutive and ras-inducible phosphorylation sites of KSR: implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression

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The protein kinase KSR interacts with 14-3-3 protein and Raf.

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Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR)

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Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization

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Kinase suppressor of Ras (KSR) is a scaffold which facilitates mitogen-activated protein kinase activation in vivo

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Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

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Phosphorylation of the kinase suppressor of ras by associated kinases

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Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin

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Raf-1-associated Protein Phosphatase 2A as a Positive Regulator of Kinase Activation

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Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions

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Regulation of Raf-1 activation and signalling by dephosphorylation

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

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A PP2A regulatory subunit positively regulates Ras-mediated signaling during Caenorhabditis elegans vulval induction

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

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

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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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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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Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits

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KSR modulates signal propagation within the MAPK cascade

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Characterization of Raf-1 activation in mitosis

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017