Two proteases with caspase-3-like activity, cathepsin B and proteasome, antagonistically control ER-stress-induced programmed cell death in Arabidopsis
© 2017 The Authors. New Phytologist © 2017 New Phytologist Trust.
| Veröffentlicht in: | The New phytologist. - 1990. - 218(2018), 3 vom: 01. Mai, Seite 1143-1155 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2018
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| Zugriff auf das übergeordnete Werk: | The New phytologist |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't ER-stress-induced death (ERSID) endoplasmic reticulum (ER)-stress plant protease proteasome subunit PBA1 tunicamycin unfolded protein response (UPR) vacuolar processing enzyme (VPE) vacuole mehr... |
| Zusammenfassung: | © 2017 The Authors. New Phytologist © 2017 New Phytologist Trust. Programmed cell death (PCD) induced by endoplasmic reticulum (ER) stress is implicated in various plant physiological processes, yet its mechanism is still elusive. An activation of caspase-3-like enzymatic activity was clearly demonstrated but the role of the two known plant proteases with caspase-3-like activity, cathepsin B and proteasome subunit PBA1, remains to be established. Both genetic downregulation and chemical inhibition were used to investigate the function of cathepsin B and PBA1 in ER-stress-induced PCD (ERSID). Transcript level and activity labelling of cathepsin B were used to assess activation. To study tonoplast rupture, a plant PCD feature, both confocal and electronic microscopies were used. Cathepsin B downregulation reduced reactive oxygen species (ROS) accumulation and ERSID without affecting the induction of the unfolded protein response (UPR), but downregulation of PBA1 increased UPR and ERSID. Tonoplast rupture was not altered in the cathepsin B mutant and cathepsin B activation was independent of vacuolar processing enzyme (VPE). VPE activity was independent of cathepsin B. ERSID is regulated positively by cathepsin B and negatively by PBA1, revealing a complex picture behind caspase-3-like activity in plants. Cathepsin B may execute its function after tonoplast rupture and works in parallel with VPE |
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| Beschreibung: | Date Completed 01.10.2019 Date Revised 30.09.2020 published: Print-Electronic CommentIn: New Phytol. 2018 May;218(3):879-881. doi: 10.1111/nph.15156. - PMID 29658638 Citation Status MEDLINE |
| ISSN: | 1469-8137 |
| DOI: | 10.1111/nph.14676 |