Activation of GCN2 in UV-irradiated cells inhibits translation (Q28591074)

Eukaryotic translation initiation factor 2 alpha kinase 4

GOA release 2020-03-11

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GOA release 2020-03-11

author

Anne-Claude Gingras

4

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Nahum Sonenberg

9

object named as

Nahum Sonenberg

1 reference

31 January 2017

David Ron

8

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Juan Jose Berlanga

object named as

Juan Jose Berlanga

5

1 reference

ORCID Public Data File 2021

author name string

Jing Deng

1

1 reference

31 January 2017

Heather P. Harding

2

1 reference

31 January 2017

Brian Raught

3

1 reference

31 January 2017

Donalyn Scheuner

6

1 reference

31 January 2017

Randal J. Kaufman

Ultraviolet radiation triggers the ribotoxic stress response in mammalian cells.

7

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31 January 2017

language of work or name

English

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publication date

6 August 2002

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31 January 2017

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31 January 2017

12

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31 January 2017

1279–1286

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31 January 2017

15

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31 January 2017

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Evolution of the two-step model for UV-mutagenesis

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Cellular responses to DNA damage

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Mitogen-activated protein kinase cascades as regulators of stress responses

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Signal transduction by the JNK group of MAP kinases

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Mutagenesis and growth delay induced in Escherichia coli by near-ultraviolet radiations

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Phosphorylation of 4E-BP1 is mediated by the p38/MSK1 pathway in response to UVB irradiation

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Initiation factor eIF2 alpha phosphorylation in stress responses and apoptosis.

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Regulation of translational initiation during cellular responses to stress

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Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast

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Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase

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Regulated translation initiation controls stress-induced gene expression in mammalian cells

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Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control

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

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Akt/Protein kinase B inhibits cell death by preventing the release of cytochrome c from mitochondria

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The mammalian ultraviolet response is triggered by activation of src tyrosine kinases

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The UV response involving the Ras signaling pathway and AP-1 transcription factors is conserved between yeast and mammals

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Translational control is required for the unfolded protein response and in vivo glucose homeostasis

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Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus

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SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase

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Ultraviolet light and osmotic stress: activation of the JNK cascade through multiple growth factor and cytokine receptors

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Sensor-less checkpoint activation?

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Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain

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7 January 2021

The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids

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Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases

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Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast

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Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2

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Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress

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Regulation of p53 in response to DNA damage

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PERK mediates cell-cycle exit during the mammalian unfolded protein response

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Ultraviolet light inhibits translation through activation of the unfolded protein response kinase PERK in the lumen of the endoplasmic reticulum

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Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase, PKR.

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

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

2271143

2271143

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference