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Two proteases with caspase-3-like activity, cathepsin B and proteasome, antagonistically control ER-stress-induced programmed cell death in Arabidopsis
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Two proteases with caspase-3-like activity, cathepsin B and proteasome, antagonistically control ER-stress-induced programmed cell death in Arabidopsis
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Two proteases with caspase-3-like activity, cathepsin B and proteasome, antagonistically control ER-stress-induced programmed cell death in Arabidopsis
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Journal Article
Two proteases with caspase-3-like activity, cathepsin B and proteasome, antagonistically control ER-stress-induced programmed cell death in Arabidopsis
2018
Overview
Programmed cell death (PCD) induced by endoplasmic reticulum (ER) stress is implicated in variousplant 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.
Publisher
New Phytologist Trust,Wiley Subscription Services, Inc,John Wiley and Sons Inc
Subject
/ Arabidopsis Proteins - metabolism
/ Caspase
/ Cysteine Endopeptidases - metabolism
/ endoplasmic reticulum (ER)‐stress
/ Endoplasmic Reticulum Stress
/ ER‐stress‐induced death (ERSID)
/ Labeling
/ mutants
/ proteasome endopeptidase complex
/ Proteasome Endopeptidase Complex - metabolism
/ Proteins
/ Rupture
/ Stresses
/ unfolded protein response (UPR)
/ vacuolar processing enzyme (VPE)
/ vacuole
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