(Q41322187)

English

Stimulus-induced uncoupling of extracellular signal-regulated kinase phosphorylation from nuclear localization is dependent on docking domain interactions

scientific article published on December 2010

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Stimulus-induced uncoupling of extracellular signal-regulated kinase phosphorylation from nuclear localization is dependent on docking domain interactions (English)

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

phosphorylation

1 reference

based on heuristic

inferred from title

Craig A McArdle

2

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

author name string

Christopher J Caunt

1

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

language of work or name

0 references

publication date

1 December 2010

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Journal of Cell Science

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

123

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Pt 24

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

4310-4320

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

Pulsatile and sustained gonadotropin-releasing hormone (GnRH) receptor signaling: does the ERK signaling pathway decode GnRH pulse frequency?

1 reference

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ERK2 but not ERK1 induces epithelial-to-mesenchymal transformation via DEF motif-dependent signaling events

1 reference

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Cell fate decisions are specified by the dynamic ERK interactome

1 reference

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ERK nuclear translocation is dimerization-independent but controlled by the rate of phosphorylation

1 reference

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KSR1 modulates the sensitivity of mitogen-activated protein kinase pathway activation in T cells without altering fundamental system outputs

1 reference

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Differential regulation and properties of MAPKs

1 reference

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Mxi2 promotes stimulus-independent ERK nuclear translocation

1 reference

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Seven-transmembrane receptor signalling and ERK compartmentalization.

1 reference

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Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells.

1 reference

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Specific inactivation and nuclear anchoring of extracellular signal-regulated kinase 2 by the inducible dual-specificity protein phosphatase DUSP5

1 reference

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Regulation of Raf-1 by direct feedback phosphorylation.

1 reference

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1 October 2017

Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways

1 reference

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Both nuclear-cytoplasmic shuttling of the dual specificity phosphatase MKP-3 and its ability to anchor MAP kinase in the cytoplasm are mediated by a conserved nuclear export signal

1 reference

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1 October 2017

A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration.

1 reference

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1 October 2017

ERK2 enters the nucleus by a carrier-independent mechanism

1 reference

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1 October 2017

Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1

1 reference

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1 October 2017

PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase

1 reference

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Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds

1 reference

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1 October 2017

Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions

1 reference

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A simple method for the rapid generation of recombinant adenovirus vectors

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Two co-existing mechanisms for nuclear import of MAP kinase: passive diffusion of a monomer and active transport of a dimer.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2995615

1 October 2017

Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry

1 reference

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1 October 2017

Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase

1 reference

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1 October 2017

A constitutively active and nuclear form of the MAP kinase ERK2 is sufficient for neurite outgrowth and cell transformation

1 reference

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1 October 2017

Growth factor-induced p42/p44 MAPK nuclear translocation and retention requires both MAPK activation and neosynthesis of nuclear anchoring proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2995615

1 October 2017

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

1 reference

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The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes

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Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase

1 reference

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1 reference

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Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Molecular interpretation of ERK signal duration by immediate early gene products

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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The nucleus, a site for signal termination by sequestration and inactivation of p42/p44 MAP kinases.

1 reference

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1 reference

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Mutations in ERK2 Binding Sites Affect Nuclear Entry

1 reference

https://pubmed.ncbi.nlm.nih.gov/21123621

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

beta-Arrestin scaffolding of the ERK cascade enhances cytosolic ERK activity but inhibits ERK-mediated transcription following angiotensin AT1a receptor stimulation

1 reference

https://pubmed.ncbi.nlm.nih.gov/21123621

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1242/JCS.076349

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

29 September 2017

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