Fine-tuning PERK signaling to control cell fate under stress

• Published in: Nature structural & molecular biology Vol. 24; no. 10; pp. 789 - 790
• Main Authors: Urra, Hery, Hetz, Claudio
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.10.2017; Nature Publishing Group
• Subjects: 631/337/470; 631/80/82; 631/80/86/2366; Animals; Apoptosis - genetics; Biochemistry; Biological Microscopy; BiP protein; Cell fate; eIF-2 Kinase - genetics; eIF-2 Kinase - metabolism; Endoplasmic reticulum; Endoplasmic Reticulum - metabolism; Feedback, Physiological; Gene Expression Regulation; Heat shock proteins; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; HEK293 Cells; Humans; Intracellular Signaling Peptides and Proteins - genetics; Intracellular Signaling Peptides and Proteins - metabolism; Life Sciences; Membrane Biology; Membrane Proteins - genetics; Membrane Proteins - metabolism; Mice; Mice, Knockout; Molecular biology; news-and-views; Phosphorylation; Protein Binding; Protein folding; Protein Structure; Proteins; Sensors; Signal Transduction; Stress; Transcription Factor CHOP - genetics; Transcription Factor CHOP - metabolism; Unfolded Protein Response
• ISSN: 1545-9993; 1545-9985
• DOI: 10.1038/nsmb.3478

PERK is a major sensor of the unfolded protein response controlling cell fate under endoplasmic reticulum (ER) stress. A new study reveals an additional step for optimal PERK signaling, involving the binding of CNPY2 to PERK's luminal domain. The PERK–CNPY2 axis was shown to enhance cell death under ER stress in vivo influence liver disease.