An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response
- 1 July 2023
- journal article
- research article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 667, 58-63
- https://doi.org/10.1016/j.bbrc.2023.05.044
Abstract
No abstract availableKeywords
Funding Information
- Noda Institute for Scientific Research
- Japan Society for the Promotion of Science London
- Japan Society for the Promotion of Science (22K19135)
This publication has 21 references indexed in Scilit:
- Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domainsProceedings of the National Academy of Sciences of the United States of America, 2013
- F-actin and a Type-II Myosin Are Required for Efficient Clustering of the ER Stress Sensor Ire1Cell Structure and Function, 2013
- Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein ResponseScience, 2011
- Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different waysMolecular Biology of the Cell, 2011
- Signalling Pathways in the Unfolded Protein Response: Development from Yeast to MammalsThe Journal of Biochemistry, 2009
- Real-Time Redox Measurements during Endoplasmic Reticulum Stress Reveal Interlinked Protein Folding FunctionsCell, 2008
- Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteinsThe Journal of cell biology, 2007
- Yeast unfolded protein response pathway regulates expression of genes for anti‐oxidative stress and for cell surface proteinsGenes to Cells, 2005
- A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1The Journal of cell biology, 2004
- Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic‐leucine zipper motif is required for the unfolded protein‐response pathwayGenes to Cells, 1996