The accumulation of unfolded protein in the endoplasmic reticulum (ER) attenuates protein
synthesis initiation through phosphorylation of the α subunit of eukaryotic translation initiation …

Stress granules (SGs) are cytoplasmic aggregates of stalled translational preinitiation
complexes that accumulate during stress. GW bodies/processing bodies (PBs) are distinct …

Most protein phosphatases have little intrinsic substrate specificity, making selective
pharmacological inhibition of specific dephosphorylation reactions a challenging problem. In a …

Tumor cell adaptation to hypoxic stress is an important determinant of malignant progression.
While much emphasis has been placed on the role of HIF‐1 in this context, the role of …

The eIF2α kinases are a family of evolutionarily conserved serine/threonine kinases that
regulate stress-induced translational arrest. Here, we demonstrate that the yeast eIF2α kinase, …

Eukaryotic cells coordinate protein-folding reactions in the endoplasmic reticulum with gene
expression in the nucleus and messenger RNA translation in the cytoplasm. As the rate of …

The progression from insulin resistance to type 2 diabetes is caused by the failure of
pancreatic β cells to produce sufficient levels of insulin to meet the metabolic demand. Recent …

Numerous stressful conditions activate kinases that phosphorylate the alpha subunit of
translation initiation factor 2 (eIF2α), thus attenuating mRNA translation and activating a gene …

The endoplasmic reticulum (ER) is the entry site into the secretory pathway for newly synthesized
proteins destined for the cell surface or released into the extracellular milieu. The study …

Nuclear factor κB (NF-κB) serves to coordinate the transcription of genes in response to
diverse environmental stresses. In this report we show that phosphorylation of the α subunit of …