Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD (Q24531859)

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English	Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD	scientific article

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instance of

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title

Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD (English)

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Joe W Ramos

4

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author name string

Hemamalini Renganathan

series ordinal

1

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Hema Vaidyanathan

series ordinal

2

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Anna Knapinska

series ordinal

3

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language of work or name

English

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publication date

15 September 2005

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published in

Biochemical Journal

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volume

390

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issue

Pt 3

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page(s)

729-35

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cites work

Protein kinase B/Akt binds and phosphorylates PED/PEA-15, stabilizing its antiapoptotic action

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PubMed Central

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24 March 2017

PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis

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24 March 2017

PED/PEA-15 gene controls glucose transport and is overexpressed in type 2 diabetes mellitus

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PubMed Central

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24 March 2017

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

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PubMed Central

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24 March 2017

Omi/HtrA2 promotes cell death by binding and degrading the anti-apoptotic protein ped/pea-15

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PubMed Central

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24 March 2017

RSK2 activity is regulated by its interaction with PEA-15

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PubMed Central

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24 March 2017

Tumor necrosis factor-related apoptosis-inducing ligand-induced death-inducing signaling complex and its modulation by c-FLIP and PED/PEA-15 in glioma cells

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PubMed Central

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24 March 2017

PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase

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PubMed Central

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24 March 2017

Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFalpha-induced apoptosis

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PubMed Central

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24 March 2017

Endothelin induces a calcium-dependent phosphorylation of PEA-15 in intact astrocytes: identification of Ser104 and Ser116 phosphorylated, respectively, by protein kinase C and calcium/calmodulin kinase II in vitro

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PubMed Central

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24 March 2017

Characterization of PEA-15, a major substrate for protein kinase C in astrocytes

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PubMed Central

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24 March 2017

The phosphoprotein protein PEA-15 inhibits Fas- but increases TNF-R1-mediated caspase-8 activity and apoptosis

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24 March 2017

Protein kinase C (PKC)-alpha activation inhibits PKC-zeta and mediates the action of PED/PEA-15 on glucose transport in the L6 skeletal muscle cells

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PubMed Central

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27 September 2017

Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism

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PubMed Central

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27 September 2017

Cancer research center hotline: PEA-15 phosphoprotein: a potential cancer drug target

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PubMed Central

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29 November 2018

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

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1199667

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29 November 2018

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1199667

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29 November 2018

Induction and intracellular regulation of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) mediated apotosis in human malignant glioma cells.

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1199667

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29 November 2018

The death effector domain of PEA-15 is involved in its regulation of integrin activation

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1199667

retrieved

29 November 2018

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ResearchGate publication ID

7824286

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Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD (Q24531859)

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Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD (Q24531859)

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