Results 41 to 50 of about 363,972 (179)

Phosphorylation of eukaryotic initiation factor-2α (eIF2α) in autophagy

open access: yes, 2020
International audienceThe integrated stress response is characterized by the phosphorylation of eukaryotic initiation factor-2α (eIF2α) on serine 51 by one out of four specific kinases (EIF2AK1 to 4).
Kepp, Oliver   +11 more
core   +1 more source

A role for eIF5A in translational control of stress‐inducible proteins in multiple myeloma cell lines

open access: yesMolecular Oncology, EarlyView.
Loss of eIF5A rewires thapsigargin‐mediated endoplasmic reticulum stress responses in multiple myeloma cells by selective translation of mRNA transcripts, consequently dampening thapsigargin‐induced unfolded protein response (UPR) activation and shifting the balance from induction of apoptosis toward cell survival and proliferation.
Demi Both   +7 more
wiley   +1 more source

ER stress-induced eIF2-alpha phosphorylation underlies sensitivity of striatal neurons to pathogenic huntingtin.

open access: yesPLoS ONE, 2014
A hallmark of Huntington's disease is the pronounced sensitivity of striatal neurons to polyglutamine-expanded huntingtin expression. Here we show that cultured striatal cells and murine brain striatum have remarkably low levels of phosphorylation of ...
Julia Leitman   +6 more
doaj   +1 more source

PKR expression is required for eIF2α phosphorylation following treatment of breast cancer cell lines with doxorubicin.

open access: yes, 2012
Breast cancer lines with reduced PKR expression (siPKR) or control cells (siControl) were treated with 2.5 µM DOX for the indicated times. Following treatment, cells were collected and western blotting using antibody specific for phosphoserine-51 eIF2α ...
Teng Hui (132560)   +5 more
core   +1 more source

Hyperosmotic stress‐induced redistribution of pre‐mRNA cleavage factor I subunits is associated with shifts in alternative polyadenylation

open access: yesFEBS Open Bio, EarlyView.
Hyperosmotic stress triggers the relocation of the CFIm complex from the nucleus to the cytoplasm. This shift creates a nuclear ‘stoichiometric bottleneck’, limiting CFIm availability for mRNA processing. Consequently, specific mRNAs like NUDT21 and DICER1 undergo targeted 3′UTR shortening, demonstrating how spatial protein dynamics drive rapid ...
Hitomi Soumiya   +2 more
wiley   +1 more source

Requirement for kinase-induced conformational change in eukaryotic initiation factor 2α (eIF2α) restricts phosphorylation of Ser51

open access: yes, 2011
As phosphorylation of eukaryotic translation initiation factor 2α (eIF2α) on Ser51 inhibits protein synthesis, cells restrict this phosphorylation to the antiviral protein kinase PKR and related eIF2α kinases. In the crystal structure of the
John J. Li   +7 more
core   +1 more source

Yeast Gcn2 retains activity following humanization of its auto‐phosphorylation region

open access: yesFEBS Open Bio, EarlyView.
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.
Reuben A. Anderson   +2 more
wiley   +1 more source

Protein synthesis attenuation by phosphorylation of eIF2α is required for the differentiation of Trypanosoma cruzi into infective forms.

open access: yesPLoS ONE, 2011
Chagas' disease is a potentially life-threatening illness caused by the unicellular protozoan parasite Trypanosoma cruzi. It is transmitted to humans by triatomine bugs where T. cruzi multiplies and differentiates in the digestive tract.
Renata R Tonelli   +3 more
doaj   +1 more source

MARK2 phosphorylates eIF2α in response to proteotoxic stress.

open access: yesPLoS Biology, 2021
The regulation of protein synthesis is essential for maintaining cellular homeostasis, especially during stress responses, and its dysregulation could underlie the development of human diseases.
Yu-Ning Lu   +7 more
doaj   +1 more source

Prion‐Like Protein LENG8‐Mediated Nucleation Drives Stress Granule Assembly

open access: yesAdvanced Science, EarlyView.
LENG8 is a newly identified stress granule (SG) nucleator required for SG assembly. Following stress, nuclear LENG8 granules disassemble, allowing LENG8 to translocate into the cytoplasm and form independent nucleation foci. These foci fuse with canonical early G3BP1/TIA1 seeds via LENG8‐TIA1 binding to drive SG maturation.
Mingxing Zhang   +6 more
wiley   +1 more source

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