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Journal ArticleDOI

eIF2 and the control of cell physiology

TLDR
While phosphorylation of eIF2 serves to impair general protein synthesis, it causes upregulation of the translation of certain specific mRNAs that encode transcription factors which can exert effects on gene expression at multiple levels.
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This article is published in Seminars in Cell & Developmental Biology.The article was published on 2005-02-01. It has received 378 citations till now. The article focuses on the topics: eIF2B & EIF4EBP1.

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Citations
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Journal ArticleDOI

Mechanisms of Cancer Cachexia

TL;DR: Tumor factors such as proteolysis-inducing factor and host factors can all induce muscle atrophy, and knowledge of the mechanisms of tissue destruction in cachexia should improve methods of treatment.
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Cellular response to endoplasmic reticulum stress: a matter of life or death.

TL;DR: What is known about the ESR in both yeast and mammals is reviewed, and recent findings on the mechanism and pathophysiological importance of ER stress-induced apoptosis are highlighted.
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Endoplasmic reticulum stress and type 2 diabetes.

TL;DR: This review examines how the UPR pathways, induced by high glucose and free fatty acids (FFAs), interact to disrupt ER function and cause β-cell dysfunction and death.
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Role of the unfolded protein response in cell death.

TL;DR: Less susceptibility to cell death upon activation of the UPR may contribute to tumor progression and drug resistance of solid tumors.
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Endoplasmic reticulum stress in health and disease

TL;DR: Recent progress suggests that ER stress and UPR play key roles in the immune response, diabetes, tumor growth under hypoxic conditions, and in some neurodegenerative diseases.
References
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Book

Translational control of gene expression

TL;DR: Origins and Principles of Translational Control, Genetic Approaches to Translation Initiation in Saccharomyces cerevisiae, and Programmed translational Frameshifting, Hopping, an
Journal ArticleDOI

Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis

TL;DR: It is demonstrated that regulation of translation through eIF2alpha phosphorylation is essential for the ER stress response and in vivo glucose homeostasis.
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Feedback Inhibition of the Unfolded Protein Response by GADD34-Mediated Dephosphorylation of eIF2α

TL;DR: Findings implicate GADD34-mediated dephosphorylation of eIF2α in a negative feedback loop that inhibits stress-induced gene expression, and that might promote recovery from translational inhibition in the unfolded protein response.
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RNA-Binding Proteins Tia-1 and Tiar Link the Phosphorylation of Eif-2α to the Assembly of Mammalian Stress Granules

TL;DR: The ability of a TIA-1 mutant lacking its RNA-binding domains to function as a transdominant inhibitor of SG formation suggests that this RNA- binding protein acts downstream of the phosphorylation of eIF-2α to promote the sequestration of untranslated mRNAs at SGs.
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EIF2AK3 , encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome

TL;DR: The results provide evidence for the role of EIF2AK3 in WRS and may provide insight into the understanding of the more common forms of diabetes and other pathologic manifestations of WRS.
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