Author
Listed:
- Noelia Pastor-Cantizano
(Michigan State University
University of Valencia)
- Evan R. Angelos
(Michigan State University
University of California Riverside)
- Cristina Ruberti
(Michigan State University
University of Milan)
- Tao Jiang
(Michigan State University
University of Florida)
- Xiaoyu Weng
(University of Texas)
- Brandon C. Reagan
(Michigan State University)
- Taslima Haque
(University of Texas
University of Michigan)
- Thomas E. Juenger
(University of Texas)
- Federica Brandizzi
(Michigan State University
Michigan State University
Michigan State University)
Abstract
Environmental and physiological situations can challenge the balance between protein synthesis and folding capacity of the endoplasmic reticulum (ER) and cause ER stress, a potentially lethal condition. The unfolded protein response (UPR) restores ER homeostasis or actuates programmed cell death (PCD) when ER stress is unresolved. The cell fate determination mechanisms of the UPR are not well understood, especially in plants. Here, we integrate genetics and ER stress profiling with natural variation and quantitative trait locus analysis of 350 natural accessions of the model species Arabidopsis thaliana. Our analyses implicate a single nucleotide polymorphism to the loss of function of the general PCD regulator BON-ASSOCIATED PROTEIN2 (BAP2) in UPR outcomes. We establish that ER stress-induced BAP2 expression is antagonistically regulated by the UPR master regulator, inositol-requiring enzyme 1 (IRE1), and that BAP2 controls adaptive UPR amplitude in ER stress and ignites pro-death mechanisms in conditions of UPR insufficiency.
Suggested Citation
Noelia Pastor-Cantizano & Evan R. Angelos & Cristina Ruberti & Tao Jiang & Xiaoyu Weng & Brandon C. Reagan & Taslima Haque & Thomas E. Juenger & Federica Brandizzi, 2024.
"Programmed cell death regulator BAP2 is required for IRE1-mediated unfolded protein response in Arabidopsis,"
Nature Communications, Nature, vol. 15(1), pages 1-17, December.
Handle:
RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-50105-6
DOI: 10.1038/s41467-024-50105-6
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