Results 11 to 20 of about 28,887 (200)

Roles of eIF2α kinases in the pathogenesis of Alzheimer’s disease [PDF]

Frontiers in Molecular Neuroscience, 2014
Cell signaling in response to an array of diverse stress stimuli converges on the phosphorylation of eukaryotic initiation factor-2α (eIF2α). Evidence is accumulating that persistent eIF2α phosphorylation at Ser51 through prolonged overactivation of ...
Masuo eOhno, Masuo eOhno
doaj   +3 more sources

Impact of eIF2α phosphorylation on the translational landscape of mouse embryonic stem cells

Cell Reports
Summary: The integrated stress response (ISR) is critical for cell survival under stress. In response to diverse environmental cues, eIF2α becomes phosphorylated, engendering a dramatic change in mRNA translation.
Mehdi Amiri, Stephen J. Kiniry, Anthony P. Possemato, Niaz Mahmood, Tayebeh Basiri, Catherine R. Dufour, Negar Tabatabaei, Qiyun Deng, Michael A. Bellucci, Keerthana Harwalkar, Matthew P. Stokes, Vincent Giguère, Randal J. Kaufman, Yojiro Yamanaka, Pavel V. Baranov, Soroush Tahmasebi, Nahum Sonenberg   +16 more
doaj   +2 more sources

Yeast Gcn2 retains activity following humanization of its auto-phosphorylation region. [PDF]

FEBS Open Bio
Using Saccharomyces cerevisiae as a model to study Gcn2 activation and regulation is limited by the lack of antibodies detecting phosphorylated Gcn2. To overcome this, we engineered Gcn2‐HsC, a yeast Gcn2 variant recognizable by commercial anti‐human phospho‐GCN2 antibodies.
Anderson RA, Schiemann AH, Sattlegger E.
europepmc   +2 more sources

Endoplasmic reticulum stress mediates radiation-induced autophagy by perk-eIF2α in caspase-3/7-deficient cells [PDF]

Oncogene, 2010
As apoptosis defects limit efficacy of anticancer agents, autophagy has been proposed as a novel strategy for radiotherapy enhancement. We previously showed that caspase-3/7 inhibition induces autophagy and promotes radiosensitivity in vitro and in vivo. Therefore, we further investigated the mechanism by which radiation triggers autophagy in caspase-3/
Kim, Kwang Woon, Moretti, Luigi, Mitchell, L.R., Jung, D.K., Lu, Bo   +4 more
openaire   +3 more sources

Glucose-stimulated Protein Synthesis in Pancreatic β-Cells Parallels an Increase in the Availability of the Translational Ternary Complex (eIF2-GTP·Met-tRNAi) and the Dephosphorylation of eIF2α [PDF]

Journal of Biological Chemistry, 2004
In pancreatic beta-cells, glucose causes a rapid increase in the rate of protein synthesis. However, the mechanism by which this occurs is poorly understood. In this report, we demonstrate, in the pancreatic beta-cell line MIN6, that glucose stimulates the recruitment of ribosomes onto the mRNA, indicative of an increase in the rate of the initiation ...
E. Gomez, M.L. Powell, I.C. Greenman, Terence Herbert   +3 more
openaire   +4 more sources

Expression of eIF2α and phospho-eIF2α.

, 2023
Huh7.5 cells were electroporated with mJFH-1 WT and DI mutant C142A, C190A and E191A RNAs, together with an NS5B GND mutant as negative control. TM: tunicamycin positive control. Cells were harvested at 72 hpe and lysed with GLB.
Shucheng Chen (1419898), Mark Harris (33805)   +1 more
core   +1 more source

The role of host eIF2α in viral infection

Virology Journal, 2020
Background eIF2α is a regulatory node that controls protein synthesis initiation by its phosphorylation or dephosphorylation. General control nonderepressible-2 (GCN2), protein kinase R-like endoplasmic reticulum kinase (PERK), double-stranded RNA (dsRNA)
Yuanzhi Liu, Mingshu Wang, Anchun Cheng, Qiao Yang, Ying Wu, Renyong Jia, Mafeng Liu, Dekang Zhu, Shun Chen, Shaqiu Zhang, Xin-Xin Zhao, Juan Huang, Sai Mao, Xumin Ou, Qun Gao, Yin Wang, Zhiwen Xu, Zhengli Chen, Ling Zhu, Qihui Luo, Yunya Liu, Yanling Yu, Ling Zhang, Bin Tian, Leichang Pan, Mujeeb Ur Rehman, Xiaoyue Chen   +26 more
doaj   +1 more source

eIF2α phosphorylation controls thermal nociception [PDF]

, 2016
A response to environmental stress is critical to alleviate cellular injury and maintain cellular homeostasis. Eukaryotic initiation factor 2 (eIF2) is a key integrator of cellular stress responses and an important regulator of mRNA translation.
Ribeiro-da-Silva, Alfredo, Cervero, Fernando, Longo, Geraldine, Pitcher, Mark H., W. Bourque, Charles, Khoutorsky, Arkady, Pawlowski, Sophie Anne, Sharif-Naeini, Reza, Mehdi Jafarnejad, Seyed, Martin, Loren, Mogil, Jeffrey S., Prager-Khoutorsky, Masha, Tahmasebi, Soroush, Sonenberg, Nahum, Gkogkas, Christos, Sorge, Robert E.   +15 more
core   +1 more source

Genetic inhibition of phosphorylation of the translation initiation factor eIF2α does not block Aβ-dependent elevation of BACE1 and APP levels or reduce amyloid pathology in a mouse model of Alzheimer's disease. [PDF]

PLoS ONE, 2014
β-site amyloid precursor protein (APP) cleaving enzyme 1 (BACE1) initiates the production of β-amyloid (Aβ), the major constituent of amyloid plaques in Alzheimer's disease (AD).
Katherine R Sadleir, William A Eimer, Randal J Kaufman, Pavel Osten, Robert Vassar   +4 more
doaj   +1 more source

PKR and GCN2 stress kinases promote an ER stress-independent eIF2α phosphorylation responsible for calreticulin exposure in melanoma cells

OncoImmunology, 2018
The immunogenic cell death (ICD) process represents a novel therapeutic approach to treat tumours, in which cytotoxic compounds promote both cancer cell death and the emission of damage-associated molecular patterns (DAMPs) from dying cells, to activate ...
Paola Giglio, Mara Gagliardi, Nicola Tumino, Fernanda Antunes, Soraya Smaili, Diego Cotella, Claudio Santoro, Roberta Bernardini, Maurizio Mattei, Mauro Piacentini, Marco Corazzari   +10 more
doaj   +1 more source