Structure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK (Q27677302)

1

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Yann Wallez

2

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Michael F Egger

3

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Małgorzata K Dobaczewska

4

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Howard Robinson

5

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Elena B Pasquale

6

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Stefan J Riedl

Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove

7

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language of work or name

English

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publication date

2013

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published in

Nature Communications

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volume

4

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page(s)

1681

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cites work

1 reference

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Phosphorylation of DCC by ERK2 is facilitated by direct docking of the receptor P1 domain to the kinase

20 March 2017

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Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs

20 March 2017

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Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain

20 March 2017

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Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase

20 March 2017

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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

20 March 2017

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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

20 March 2017

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The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue

20 March 2017

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Nuclear localization and regulation of erk- and rsk-encoded protein kinases

20 March 2017

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20 March 2017

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20 March 2017

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20 March 2017

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Likelihood-enhanced fast rotation functions

20 March 2017

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The conformational plasticity of protein kinases

20 March 2017

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The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway.

20 March 2017

1 reference

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PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase

20 March 2017

1 reference

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Mammalian MAP kinase signalling cascades

20 March 2017

1 reference

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PEA-15 is inhibited by adenovirus E1A and plays a role in ERK nuclear export and Ras-induced senescence

20 March 2017

1 reference

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

20 March 2017

1 reference

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

20 March 2017

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Coordinating ERK/MAPK signalling through scaffolds and inhibitors

20 March 2017

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Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases

7 April 2017

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Phosphorylation is the switch that turns PEA-15 from tumor suppressor to tumor promoter

7 April 2017

1 reference

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Three-dimensional docking in the MAPK p38α.

29 September 2017

1 reference

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Targeting the MAPK-RAS-RAF signaling pathway in cancer therapy

29 September 2017

1 reference

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PEA15 impairs cell migration and correlates with clinical features predicting good prognosis in neuroblastoma

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

PEA-15 potentiates H-Ras-mediated epithelial cell transformation through phospholipase D

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

Large-scale discovery of ERK2 substrates identifies ERK-mediated transcriptional regulation by ETV3.

29 September 2017

1 reference

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Examining docking interactions on ERK2 with modular peptide substrates

29 September 2017

1 reference

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Cell fate decisions are specified by the dynamic ERK interactome

29 September 2017

1 reference

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Essential role of ERK dimers in the activation of cytoplasmic but not nuclear substrates by ERK-scaffold complexes

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

Phospho-ERK staining is a poor indicator of the mutational status of BRAF and NRAS in human melanoma.

29 September 2017

1 reference

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Unique MAP Kinase binding sites

29 September 2017

1 reference

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The PEA-15/PED protein protects glioblastoma cells from glucose deprivation-induced apoptosis via the ERK/MAP kinase pathway.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

PEA-15 inhibits tumor cell invasion by binding to extracellular signal-regulated kinase 1/2.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis

29 September 2017

1 reference

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High yield bacterial expression of active c-Abl and c-Src tyrosine kinases

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

ERK2 enters the nucleus by a carrier-independent mechanism

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3640864

The death effector domain protein PEA-15 prevents nuclear entry of ERK2 by inhibiting required interactions.

2 June 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS2687

PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS2687

Expression of phosphoprotein enriched in astrocytes 15 kDa (PEA-15) in astrocytic tumors: a novel approach of correlating malignancy grade and prognosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS2687

The anti-apoptotic protein PEA-15 is a tight binding inhibitor of ERK1 and ERK2, which blocks docking interactions at the D-recruitment site.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS2687

Docking motif interactions in MAP kinases revealed by hydrogen exchange mass spectrometry

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS2687

Evidence for existence of a nuclear pore complex-mediated, cytosol-independent pathway of nuclear translocation of ERK MAP kinase in permeabilized cells.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS2687

ERK dimers and scaffold proteins: unexpected partners for a forgotten (cytoplasmic) task.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS2687

PEA-15 inhibits tumorigenesis in an MDA-MB-468 triple-negative breast cancer xenograft model through increased cytoplasmic localization of activated extracellular signal-regulated kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS2687

Docking interactions induce exposure of activation loop in the MAP kinase ERK2

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23575685

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NCOMMS2687

1 reference

Dimensions Publication ID

ADS bibcode

2013NatCo...4.1681M

0 references

1037697601

0 references

1 reference

1 reference

PubMed publication ID

23575685

1 reference