Fortilin binds IRE1α and prevents ER stress from signaling apoptotic cell death

• Published in: Nature communications Vol. 8; no. 1; pp. 18 - 16
• Main Authors: Pinkaew, Decha, Chattopadhyay, Abhijnan, King, Matthew D., Chunhacha, Preedakorn, Liu, Zhihe, Stevenson, Heather L., Chen, Yanjie, Sinthujaroen, Patuma, McDougal, Owen M., Fujise, Ken
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 26.05.2017; Nature Portfolio
• Subjects: 631/337/470/1463; 631/45/470/1463; Activating Transcription Factor 6 - genetics; Activating Transcription Factor 6 - metabolism; Animals; Apoptosis; Biomarkers, Tumor - genetics; Biomarkers, Tumor - metabolism; Cell Line, Tumor; eIF-2 Kinase - genetics; eIF-2 Kinase - metabolism; Endoplasmic Reticulum - genetics; Endoplasmic Reticulum - metabolism; Endoplasmic Reticulum Stress - genetics; Endoribonucleases - genetics; Endoribonucleases - metabolism; Epithelial Cells - cytology; Epithelial Cells - metabolism; Gene Expression Regulation; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; Humanities and Social Sciences; Humans; Mice; multidisciplinary; Osteoblasts - cytology; Osteoblasts - metabolism; Protein-Serine-Threonine Kinases - genetics; Protein-Serine-Threonine Kinases - metabolism; Science; Science (multidisciplinary); Signal Transduction; Transduction, Genetic; Unfolded Protein Response

The endoplasmic reticulum, the cytoplasmic organelle that matures a massive amount of nascent secretory polypeptides, is particularly sensitive to stress. Endoplasmic reticulum stress causes unfolded proteins to populate the organelle, eliciting the unfolded protein response. During the unfolded pro...