MEK1 binds directly to betaarrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization (Q37160913)

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scientific article published on 19 January 2009

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English	MEK1 binds directly to betaarrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization	scientific article published on 19 January 2009

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

MEK1 binds directly to betaarrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization (English)

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

phosphorylation

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Miles D. Houslay

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Miles D Houslay

8

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author name string

Dong Meng

1

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Martin J Lynch

2

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Europe PubMed Central

PMC publication ID

18 August 2017

Elaine Huston

3

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Michael Beyermann

4

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Jenny Eichhorst

5

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

David R Adams

6

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Enno Klussmann

7

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

George S Baillie

9

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Europe PubMed Central

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18 August 2017

language of work or name

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publication date

19 January 2009

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Europe PubMed Central

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18 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

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18 August 2017

284

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Europe PubMed Central

PMC publication ID

18 August 2017

17

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Europe PubMed Central

PMC publication ID

18 August 2017

11425-11435

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Beta-arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

Functional specialization of beta-arrestin interactions revealed by proteomic analysis

1 reference

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6 September 2017

Physiological roles of G protein-coupled receptor kinases and arrestins

1 reference

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6 September 2017

Beta-arrestins and cell signaling

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

Mapping binding sites for the PDE4D5 cAMP-specific phosphodiesterase to the N- and C-domains of beta-arrestin using spot-immobilized peptide arrays

1 reference

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6 September 2017

Mitogen activated protein kinase inhibitors: where are we now and where are we going?

1 reference

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6 September 2017

Scanning peptide array analyses identify overlapping binding sites for the signalling scaffold proteins, beta-arrestin and RACK1, in cAMP-specific phosphodiesterase PDE4D5.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

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The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

1 reference

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Transduction of receptor signals by beta-arrestins

1 reference

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Mitogen-activated protein kinases and asthma

1 reference

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6 September 2017

beta-arrestins: traffic cops of cell signaling

1 reference

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6 September 2017

Remodelling of the PDE4 cAMP phosphodiesterase isoform profile upon monocyte-macrophage differentiation of human U937 cells.

1 reference

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The new face of active receptor bound arrestin attracts new partners

1 reference

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6 September 2017

beta-Arrestin-mediated PDE4 cAMP phosphodiesterase recruitment regulates beta-adrenoceptor switching from Gs to Gi

1 reference

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6 September 2017

Docking interactions in the mitogen-activated protein kinase cascades

1 reference

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6 September 2017

Regulation of arrestin-3 phosphorylation by casein kinase II

1 reference

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6 September 2017

Arresting developments in heptahelical receptor signaling and regulation

1 reference

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6 September 2017

Pharmacological inhibitors of MAPK pathways.

1 reference

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6 September 2017

Beta-Arrestins: new roles in regulating heptahelical receptors' functions

1 reference

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6 September 2017

Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation

1 reference

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6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

beta-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

A conserved docking motif in MAP kinases common to substrates, activators and regulators

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes

1 reference

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6 September 2017

Clathrin-mediated Endocytosis of the β-Adrenergic Receptor Is Regulated by Phosphorylation/Dephosphorylation of β-Arrestin1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670148

6 September 2017

A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function

1 reference

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G-protein-coupled receptors: regulatory role of receptor kinases and arrestin proteins

1 reference

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Mutations of beta-arrestin 2 that limit self-association also interfere with interactions with the beta2-adrenoceptor and the ERK1/2 MAPKs: implications for beta2-adrenoceptor signalling via the ERK1/2 MAPKs

1 reference

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Isoform-selective susceptibility of DISC1/phosphodiesterase-4 complexes to dissociation by elevated intracellular cAMP levels.

1 reference

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Phosphodiesterase-4 influences the PKA phosphorylation status and membrane translocation of G-protein receptor kinase 2 (GRK2) in HEK-293beta2 cells and cardiac myocytes.

1 reference

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RNA silencing identifies PDE4D5 as the functionally relevant cAMP phosphodiesterase interacting with beta arrestin to control the protein kinase A/AKAP79-mediated switching of the beta2-adrenergic receptor to activation of ERK in HEK293B2 cells.

1 reference

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1 reference

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The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins

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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3 September 2018

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1 reference

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3 September 2018

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1 reference

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

1 reference

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12 December 2020

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10.1074/JBC.M806395200

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

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