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Eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa

eIF2alpha
The translation initiation factor EIF2 catalyzes the first regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA to 40S ribosomal subunits. Binding occurs as a ternary complex of methionyl-tRNA, EIF2, and GTP. EIF2 is composed of 3 nonidentical subunits, the 36-kD EIF2-alpha subunit (EIF2S1), the 38-kD EIF2-beta subunit (EIF2S2; MIM 603908), and the 52-kD EIF2-gamma subunit (EIF2S3; MIM 300161). The rate of formation of the ternary complex is modulated by the phosphorylation state of EIF2-alpha (Ernst et al., 1987 [PubMed 2948954]).[supplied by OMIM, Feb 2010] (from NCBI)
Top mentioned proteins: PKR, ACID, CAN, V1a, CHOP
Papers on eIF2alpha
Impairment of stress granule assembly via inhibition of the eIF2alpha phosphorylation sensitizes glioma cells to chemotherapeutic agents.
New
Barcelos et al., Belo Horizonte, Brazil. In J Neurooncol, Feb 2016
UNASSIGNED: Malignant gliomas are a lethal type of brain tumors that poorly respond to chemotherapeutic drugs.
Intrarenal Renin-Angiotensin System Mediates Fatty Acid-Induced ER Stress in the Kidney.
New
Wang et al., Denver, United States. In Am J Physiol Renal Physiol, Jan 2016
The AT1R blocker valsartan or renin inhibitor aliskiren dramatically suppressed PA-induced upregulation of BiP, CHOP, IRE1α, p-eIF2alpha, and ATF4 in HK2 cells.
A Drosophila Reporter for the Translational Activation of ATF4 Marks Stressed Cells during Development.
Kang et al., Seoul, South Korea. In Plos One, 2014
ATF4 is a transcription factor whose mRNA translation is stimulated in response to stress-activated eIF2alpha kinases.
Guanabenz Treatment Accelerates Disease in a Mutant SOD1 Mouse Model of ALS.
Perrin et al., Cambridge, United States. In Plos One, 2014
Stress induced phosphorylation of the eIF2 alpha subunit by eukaryotic translation initiation factor 2-alpha kinase 3 Perk activates the UPR.
Inhibition of palmitate-induced GADD34 expression augments apoptosis in mouse insulinoma cells (MIN6).
Ortsäter et al., Stockholm, Sweden. In Cell Biochem Funct, 2014
In the present study, we have used small interfering RNA in order to knockdown GADD34 expression in insulin-producing MIN6 cells prior to induction of ER stress by palmitate and evaluated its consequences on RNA-activated protein kinase-like ER-localized eIF2alpha kinase (PERK) signalling and apoptosis.
A game of survival: herpesvirus strategies of autophagy manipulation.
Review
Cymerys et al., Warsaw, Poland. In Postepy Hig Med Dosw (online), 2013
Induction of autophagy during viral infections is mediated by different regulatory pathways, but the biggest participation belongs to PKR and eIF2alpha.
[Endoplasmic reticulum-mediated integrated stress response].
Review
Liu et al., Beijing, China. In Sheng Li Ke Xue Jin Zhan, 2013
Integrated stress response (ISR) is a high conserved cell adaptive response, which is induced by oxidative stress, deprivation of acid aminos, and endoplasmic reticulum (ER) stress through eukaryotic translation initiator factor 2alpha (eIF2alpha) pathway.
Nanosecond pulsed electric fields act as a novel cellular stress that induces translational suppression accompanied by eIF2α phosphorylation and 4E-BP1 dephosphorylation.
GeneRIF
Yano et al., Kumamoto, Japan. In Exp Cell Res, 2012
Exposure of HeLa S3 cells to nsPEFs quickly induced phosphorylation of eIF2alpha, activation of its upstream stress-responsive kinases, PERK and GCN2, and translational suppression.
Hydrogen peroxide induces stress granule formation independent of eIF2α phosphorylation.
GeneRIF
Anderson et al., Boston, United States. In Biochem Biophys Res Commun, 2012
The assembly of H(2)O(2)-induced stress granule (SG) is independent of the phosphorylation of eIF2alpha, a major trigger of SG assembly, but requires remodeling of the cap-binding eIF4F complex.
Oxidative stress increases BACE1 protein levels through activation of the PKR-eIF2α pathway.
GeneRIF
Hugon et al., Paris, France. In Biochim Biophys Acta, 2012
findings provide a new translational regulation of BACE1, under the control of double-stranded RNA dependant protein kinase in oxidative stress, where eIF2-alpha phosphorylation regulates BACE1 protein expression
Protein tyrosine phosphatase 1B deficiency potentiates PERK/eIF2α signaling in brown adipocytes.
GeneRIF
Haj et al., Davis, United States. In Plos One, 2011
PTP1B deficiency modulates PERK-eIF2alpha phosphorylation and protein synthesis
RNA granules: the good, the bad and the ugly.
Review
Boccaccio et al., Buenos Aires, Argentina. In Cell Signal, 2011
PBs are constitutive, but respond to stimuli that affect mRNA translation and decay, whereas SGs are specifically induced upon cellular stress, which triggers a global translational silencing by several pathways, including phosphorylation of the key translation initiation factor eIF2alpha, and tRNA cleavage among others.
The role of PKR/eIF2α signaling pathway in prognosis of non-small cell lung cancer.
GeneRIF
Pataer et al., Chongqing, China. In Plos One, 2010
Reduced EIF-2alpha is associated with non-small cell lung cancer.
Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling.
Impact
Tabas et al., New York City, United States. In Nat Cell Biol, 2009
TLR engagement did not suppress phosphorylation of PERK or eIF-2alpha, which are upstream of CHOP, but phospho-eIF-2alpha failed to promote translation of the CHOP activator ATF4.
Beta testing the antioxidant function of eIF2alpha phosphorylation in diabetes prevention.
Impact
Anthony et al., Indianapolis, United States. In Cell Metab, 2009
In this issue of Cell Metabolism, Kaufman and colleagues (Back et al., 2009) elegantly demonstrate that appropriate regulation of eIF2alpha phosphorylation improves glucose tolerance and beta cell viability by preventing the lethal buildup of oxidative damage due to unregulated synthesis, trafficking, and misfolding of proteins.
Translation attenuation through eIF2alpha phosphorylation prevents oxidative stress and maintains the differentiated state in beta cells.
Impact
GeneRIF
Kaufman et al., Ann Arbor, United States. In Cell Metab, 2009
The phosphorylation of eIF2alpha attenuates mRNA translation, prevents oxidative stress, and optimizes ER protein folding to support insulin production.
Protein kinase R reveals an evolutionary model for defeating viral mimicry.
Impact
Malik et al., Seattle, United States. In Nature, 2009
Poxviruses encode K3L, a mimic of eIF2alpha, which is the substrate of protein kinase R (PKR), an important component of innate immunity in vertebrates.
Translational regulatory mechanisms in synaptic plasticity and memory storage.
Review
Richter et al., Houston, United States. In Prog Mol Biol Transl Sci, 2008
In this chapter, we review the mechanisms by which certain translational regulators including eIF2alpha, 4E-BP, S6K, and CPEB control long-term synaptic plasticity and memory consolidation and their involvement in neurologic disease.
ER stress in Alzheimer's disease: a novel neuronal trigger for inflammation and Alzheimer's pathology.
Review
Ojala et al., Kuopio, Finland. In J Neuroinflammation, 2008
The most potent pathways are IRE1-TRAF2, PERK-eIF2alpha, PERK-GSK-3, ATF6-CREBH, as well as inflammatory caspase-induced signaling pathways.
Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice.
Impact
Ron et al., New York City, United States. In Cell Metab, 2008
In this study, enforced expression of a translation initiation factor 2alpha (eIF2alpha)-specific phosphatase, GADD34, was used to selectively compromise signaling in the eIF2(alphaP)-dependent arm of the ER unfolded protein response in liver of transgenic mice.
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