Bax inhibitor-1: a highly conserved endoplasmic reticulum-resident cell death suppressor

Ishikawa, Toshiki; Watanabe, Naohide; Nagano, Minoru; Kawai‐Yamada, Maki; Lam, Eric

doi:10.1038/cdd.2011.59

Cited by 121 publications

(97 citation statements)

References 75 publications

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“…It was found that BI-1 resulted in attenuation of cell death induced by biotic and abiotic stresses [8]. In our system the SlBI-1 gene was up-regulated transiently but very significantly in the roots but not in the leaves under sublethal stress evoked by 0.1 mM SA.…”

Section: Acta Biologica Hungarica 67 2016mentioning

confidence: 67%

Salicylic acid induced cysteine protease activity during programmed cell death in tomato plants

Kovács¹,

Poór²,

Szepesi³

et al. 2016

Acta Biologica Hungarica

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The hypersensitive response (HR), a type of programmed cell death (PCD) during biotic stress is mediated by salicylic acid (SA). The aim of this work was to reveal the role of proteolysis and cysteine proteases in the execution of PCD in response of SA. Tomato plants were treated with sublethal (0.1 mM) and lethal (1 mM) SA concentrations through the root system. Treatment with 1 mM SA increased the electrolyte leakage and proteolytic activity and reduced the total protein content of roots after 6 h, while the proteolytic activity did not change in the leaves and in plants exposed to 0.1 mM SA. The expression of the papain-type cysteine protease SlCYP1, the vacuolar processing enzyme SlVPE1 and the tomato metacaspase SlMCA1 was induced within the first three hours in the leaves and after 0.5 h in the roots in the presence of 1 mM SA but the transcript levels did not increase significantly at sublethal SA. The Bax inhibitor-1 (SlBI-1), an antiapoptotic gene was over-expressed in the roots after SA treatments and it proved to be transient in the presence of sublethal SA. Protease inhibitors, SlPI2 and SlLTC were upregulated in the roots by sublethal SA but their expression remained low at 1 mM SA concentration. It is concluded that in contrast to leaves the SA-induced PCD is associated with increased proteolytic activity in the root tissues resulting from a fast up-regulation of specific cysteine proteases and down-regulation of protease inhibitors.

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Section: Acta Biologica Hungarica 67 2016mentioning

confidence: 67%

Salicylic acid induced cysteine protease activity during programmed cell death in tomato plants

Kovács¹,

Poór²,

Szepesi³

et al. 2016

Acta Biologica Hungarica

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“…Conversely, BCL-2 can inhibit apoptosis through sequestration of BH3-only proteins such as BAD, BIM, Noxa, and Puma (Cheng et al 2001). ER Ca 2þ levels are also regulated by BI-1, an ER resident transmembrane cell death suppressor protein that interacts with BCL-2 and BCL-X L (Ishikawa et al 2011). Overexpression of BI-1 decreases the ER Ca 2þ concentration while BI-1 knockdown increases ER Ca 2þ concentrations (Chae et al 2004).…”

Section: Apoptosismentioning

confidence: 99%

Xenobiotic Perturbation of ER Stress and the Unfolded Protein Response

2013

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The proper folding, assembly, and maintenance of cellular proteins is a highly regulated process and is critical for cellular homeostasis. Multiple cellular compartments have adapted their own systems to ensure proper protein folding, and quality control mechanisms are in place to manage stress due to the accumulation of unfolded proteins. When the accumulation of unfolded proteins exceeds the capacity to restore homeostasis, these systems can result in a cell death response. Unfolded protein accumulation in the endoplasmic reticulum (ER) leads to ER stress with activation of the unfolded protein response (UPR) governed by the activating transcription factor 6 (ATF6), inositol requiring enzyme-1 (IRE1), and PKR-like endoplasmic reticulum kinase (PERK) signaling pathways. Many xenobiotics have been shown to influence ER stress and UPR signaling with either pro-survival or pro-death features. The ultimate outcome is dependent on many factors including the mechanism of action of the xenobiotic, concentration of xenobiotic, duration of exposure (acute vs. chronic), cell type affected, nutrient levels, oxidative stress, state of differentiation, and others. Assessing perturbations in activation or inhibition of ER stress and UPR signaling pathways are likely to be informative parameters to measure when analyzing mechanisms of action of xenobiotic-induced toxicity.

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“…The results of these studies indicate that plant BI-1 is potentially useful for engineering stress-tolerant plants. However, little is known about the mode of action of BI-1 in the cell death regulatory pathway (Ishikawa et al, 2011). While overexpression systems sometimes include artificial or offsite effects, the observation that BI-1 overexpression improves stress tolerance suggests the importance of dissecting plants overexpressing it to further address the molecular basis of BI-1 function and cell death and stress tolerance management.…”

mentioning

confidence: 99%

Overexpression of BAX INHIBITOR-1 Links Plasma Membrane Microdomain Proteins to Stress

et al. 2015

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BAX INHIBITOR-1 (BI-1) is a cell death suppressor widely conserved in plants and animals. Overexpression of BI-1 enhances tolerance to stress-induced cell death in plant cells, although the molecular mechanism behind this enhancement is unclear. We recently found that Arabidopsis (Arabidopsis thaliana) BI-1 is involved in the metabolism of sphingolipids, such as the synthesis of 2-hydroxy fatty acids, suggesting the involvement of sphingolipids in the cell death regulatory mechanism downstream of BI-1. Here, we show that BI-1 affects cell death-associated components localized in sphingolipid-enriched microdomains of the plasma membrane in rice (Oryza sativa) cells. The amount of 2-hydroxy fatty acid-containing glucosylceramide increased in the detergent-resistant membrane (DRM; a biochemical counterpart of plasma membrane microdomains) fraction obtained from BI-1-overexpressing rice cells. Comparative proteomics analysis showed quantitative changes of DRM proteins in BI-1-overexpressing cells. In particular, the protein abundance of FLOTILLIN HOMOLOG (FLOT) and HYPERSENSITIVE-INDUCED REACTION PROTEIN3 (HIR3) markedly decreased in DRM of BI-1-overexpressing cells. Loss-of-function analysis demonstrated that FLOT and HIR3 are required for cell death by oxidative stress and salicylic acid, suggesting that the decreased levels of these proteins directly contribute to the stress-tolerant phenotypes in BI-1-overexpressing rice cells. These findings provide a novel biological implication of plant membrane microdomains in stress-induced cell death, which is negatively modulated by BI-1 overexpression via decreasing the abundance of a set of key proteins involved in cell death.

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Bax inhibitor-1: a highly conserved endoplasmic reticulum-resident cell death suppressor

Cited by 121 publications

References 75 publications

Salicylic acid induced cysteine protease activity during programmed cell death in tomato plants

Salicylic acid induced cysteine protease activity during programmed cell death in tomato plants

Xenobiotic Perturbation of ER Stress and the Unfolded Protein Response

Overexpression of BAX INHIBITOR-1 Links Plasma Membrane Microdomain Proteins to Stress

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