Modulation of the eukaryotic initiation factor 2 alpha-subunit kinase PERK by tyrosine phosphorylation (Q40052972)

16 September 2017

title

Modulation of the eukaryotic initiation factor 2 alpha-subunit kinase PERK by tyrosine phosphorylation (English)

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16 September 2017

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6

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16 September 2017

Heather P Harding

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author name string

Qiaozhu Su

1

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16 September 2017

Shuo Wang

2

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16 September 2017

Hong Qing Gao

3

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16 September 2017

Shirin Kazemi

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16 September 2017

Antonis E Koromilas

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16 September 2017

language of work or name

English

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publication date

12 November 2007

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Journal of Biological Chemistry

16 September 2017

published in

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16 September 2017

volume

283

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16 September 2017

issue

1

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16 September 2017

page(s)

469-475

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Translation factors: in sickness and in health

16 September 2017

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Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase

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Interferons induce tyrosine phosphorylation of the eIF2alpha kinase PKR through activation of Jak1 and Tyk2.

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Perk is essential for translational regulation and cell survival during the unfolded protein response

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Resistance to vesicular stomatitis virus infection requires a functional cross talk between the eukaryotic translation initiation factor 2alpha kinases PERK and PKR

21 January 2018

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Functional characterization of pkr gene products expressed in cells from mice with a targeted deletion of the N terminus or C terminus domain of PKR.

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Murine embryonic fibroblasts lacking TC-PTP display delayed G1 phase through defective NF-kappaB activation

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Dominant negative function by an alternatively spliced form of the interferon-inducible protein kinase PKR.

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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

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Enhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKR

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Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2.

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Control of alpha subunit of eukaryotic translation initiation factor 2 (eIF2 alpha) phosphorylation by the human papillomavirus type 18 E6 oncoprotein: implications for eIF2 alpha-dependent gene expression and cell death

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Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells

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The catalytic activity of the eukaryotic initiation factor-2alpha kinase PKR is required to negatively regulate Stat1 and Stat3 via activation of the T-cell protein-tyrosine phosphatase

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A chaperone-dependent GSK3beta transitional intermediate mediates activation-loop autophosphorylation

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HIV-1 Tat directly interacts with the interferon-induced, double-stranded RNA-dependent kinase, PKR

21 January 2018

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The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR

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Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B.

21 January 2018

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Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR

21 January 2018

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Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

21 January 2018

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The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro

21 January 2018

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Mechanistic Link between PKR Dimerization, Autophosphorylation, and eIF2α Substrate Recognition

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Higher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKR

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M704612200

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16 September 2017

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