Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2. (Q34427458)

2 August 2017

title

Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2. (English)

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2 August 2017

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Antonina Roll-Mecak

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Stephen K Burley

object named as

Stephen K Burley

5

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author name string

Anil K Padyana

1

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2 August 2017

Hongfang Qiu

2

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2 August 2017

Alan G Hinnebusch

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2 August 2017

language of work or name

English

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publication date

17 June 2005

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Journal of Biological Chemistry

2 August 2017

published in

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2 August 2017

volume

280

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2 August 2017

issue

32

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2 August 2017

page(s)

29289-29299

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Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform cortex.

2 August 2017

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

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Ribosome-binding Domain of Eukaryotic Initiation Factor-2 Kinase GCN2 Facilitates Translation Control

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Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain

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Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions

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Evidence that GCN1 and GCN20, Translational Regulators of GCN4, Function on Elongating Ribosomes in Activation of eIF2α Kinase GCN2

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21 January 2018

Identifiers

DOI

10.1074/JBC.M504096200

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2 August 2017

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