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Multiple mechanisms activate GCN2 eIF2 kinase in response to diverse stress conditions.
Misra, Jagannath; Carlson, Kenneth R; Spandau, Dan F; Wek, Ronald C.
Afiliación
  • Misra J; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, MS4067 Indianapolis, Indiana 46202, USA.
  • Carlson KR; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, MS4067 Indianapolis, Indiana 46202, USA.
  • Spandau DF; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, MS4067 Indianapolis, Indiana 46202, USA.
  • Wek RC; Department of Dermatology, Indiana University School of Medicine, 635 Barnhill Drive, MS4067 Indianapolis, Indiana 46202, USA.
Nucleic Acids Res ; 52(4): 1830-1846, 2024 Feb 28.
Article en En | MEDLINE | ID: mdl-38281137
ABSTRACT
Diverse environmental insults induce the integrated stress response (ISR), which features eIF2 phosphorylation and translational control that serves to restore protein homeostasis. The eIF2 kinase GCN2 is a first responder in the ISR that is activated by amino acid depletion and other stresses not directly related to nutrients. Two mechanisms are suggested to trigger an ordered process of GCN2 activation during stress GCN2 monitoring stress via accumulating uncharged tRNAs or by stalled and colliding ribosomes. Our results suggest that while ribosomal collisions are indeed essential for GCN2 activation in response to translational elongation inhibitors, conditions that trigger deacylation of tRNAs activate GCN2 via its direct association with affected tRNAs. Both mechanisms require the GCN2 regulatory domain related to histidyl tRNA synthetases. GCN2 activation by UV irradiation features lowered amino acids and increased uncharged tRNAs and UV-induced ribosome collisions are suggested to be dispensable. We conclude that there are multiple mechanisms that activate GCN2 during diverse stresses.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Serina-Treonina Quinasas Límite: Humans Idioma: En Revista: Nucleic Acids Res Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Serina-Treonina Quinasas Límite: Humans Idioma: En Revista: Nucleic Acids Res Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido