ArticleThe Journal of biological chemistry2011
Bifunctional apoptosis regulator (BAR), an endoplasmic reticulum (ER)-associated E3 ubiquitin ligase, modulates BI-1 protein stability and function in ER Stress.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- The ubiquitin E3 ligase BFAR promotes degradation of PNPLA3.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanisms of substrate processing during ER-associated protein degradation.Nature reviews. Molecular cell biology · 2023Review
- TMBIM6 promotes diabetic tubular epithelial cell survival and albumin endocytosis by inhibiting the endoplasmic reticulum stress sensor, IRE1α.Molecular biology reports · 2022Article
- The Roles of the Ubiquitin-Proteasome System in the Endoplasmic Reticulum Stress Pathway.International journal of molecular sciences · 2021Review
- BAX inhibitor-1: between stress and survival.The FEBS journal · 2020Review
- Adenoviral TMBIM6 vector attenuates ER-stress-induced apoptosis in a neonatal hypoxic-ischemic rat model.Disease models & mechanisms · 2019Article
- Proteostasis In The Endoplasmic Reticulum: Road to Cure.Cancers · 2019Review
- TMBIM protein family: ancestral regulators of cell death.Oncogene · 2015Review
- Regulatory crosstalk within the mammalian unfolded protein response.Cellular and molecular life sciences : CMLS · 2014Review
- ER stress-induced cell death mechanisms.Biochimica et biophysica acta · 2013Review
- E3 ubiquitin ligases in protein quality control mechanism.Molecular neurobiology · 2012Review
- Replication-independent expression of anti-apoptosis marker genes in human peripheral blood mononuclear cells infected with the wild-type HIV-1 and reverse transcriptase variants.Viral immunology · 2012Article
- The unfolded protein response: controlling cell fate decisions under ER stress and beyond.Nature reviews. Molecular cell biology · 2012Review
- Antiviral activity of a small molecule deubiquitinase inhibitor occurs via induction of the unfolded protein response.PLoS pathogens · 2012Article
- The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function.Membranes · 2011Article
- Bax inhibitor 1 in apoptosis and disease.Oncogene · 2011Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Accumulation of misfolded proteins in the endoplasmic reticulum (ER) causes ER stress and activates inositol-requiring protein-1 (IRE1), among other ER-associated signaling proteins of the unfolded protein response (UPR) in mammalian cells. IRE1 signaling becomes attenuated under prolonged ER stress. The mechanisms by which this occurs are not well understood. An ER resident protein, Bax inhibitor-1 (BI-1), interacts with IRE1 and directly inhibits IRE1 activity. However, little is known about regulation of the BI-1 protein. We show here that bifunctional apoptosis regulator (BAR) functions as an ER-associated RING-type E3 ligase, interacts with BI-1, and promotes proteasomal degradation of BI-1. Overexpression of BAR reduced BI-1 protein levels in a RING-dependent manner. Conversely, knockdown of endogenous BAR increased BI-1 protein levels and enhanced inhibition of IRE1 signaling during ER stress. We also found that the levels of endogenous BAR were reduced under prolonged ER stress. Our findings suggest that post-translational regulation of the BI-1 protein by E3 ligase BAR contributes to the dynamic control of IRE1 signaling during ER stress.
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Registered trials
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