Cargando…
Phosphorylation of the translation initiation factor eIF2α at serine 51 determines the cell fate decisions of Akt in response to oxidative stress
Phosphorylation of the α subunit of the translation initiation factor eIF2 at serine 51 (eIF2αP) is a master regulator of cell adaptation to various forms of stress with implications in antitumor treatments with chemotherapeutic drugs. Herein, we demonstrate that genetic loss of the eIF2α kinases PE...
Autores principales: | Rajesh, K, Krishnamoorthy, J, Kazimierczak, U, Tenkerian, C, Papadakis, A I, Wang, S, Huang, S, Koromilas, A E |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4669752/ https://www.ncbi.nlm.nih.gov/pubmed/25590801 http://dx.doi.org/10.1038/cddis.2014.554 |
Ejemplares similares
-
The eIF2α serine 51 phosphorylation-ATF4 arm promotes HIPPO signaling and cell death under oxidative stress
por: Rajesh, Kamindla, et al.
Publicado: (2016) -
Phosphorylation of eIF2α at Serine 51 Is an Important Determinant of Cell Survival and Adaptation to Glucose Deficiency
por: Muaddi, Hala, et al.
Publicado: (2010) -
Downregulation of PERK activity and eIF2α serine 51 phosphorylation by mTOR complex 1 elicits pro-oxidant and pro-death effects in tuberous sclerosis-deficient cells
por: Krishnamoorthy, Jothilatha, et al.
Publicado: (2018) -
eIF2α phosphorylation bypasses premature senescence caused by oxidative stress and pro-oxidant antitumor therapies
por: Rajesh, Kamindla, et al.
Publicado: (2013) -
Evidence for eIF2α phosphorylation-independent effects of GSK2656157, a novel catalytic inhibitor of PERK with clinical implications
por: Krishnamoorthy, Jothilatha, et al.
Publicado: (2014)