ArticleProceedings of the National Academy of Sciences of the United States of America2019
Bax inhibitor 1 is a γ-secretase-independent presenilin-binding protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Lisinopril activates BI1 to reprogram lipid metabolism and restore autophagy in ALS.Communications biology · 2026Article
- BI1 Activates Autophagy and Mediates TDP43 to Regulate ALS Pathogenesis.Molecular neurobiology · 2025Article
- A multi-cohort study of the hippocampal radiomics model and its associated biological changes in Alzheimer's Disease.Translational psychiatry · 2024Article
- Genome-wide transcriptome analysis identifies novel dysregulated genes implicated in Alzheimer's pathology.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2020Article
- [Progress on loss-of-function hypothesis of presenilin-1 mutations in Alzheimer diseases].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2020Article
- TMBIM6/BI-1 contributes to cancer progression through assembly with mTORC2 and AKT activation.Nature communications · 2020Article
- BAX inhibitor-1: between stress and survival.The FEBS journal · 2020Review
- Bax inhibitor 1 preserves mitochondrial homeostasis in acute kidney injury through promoting mitochondrial retention of PHB2.Theranostics · 2020Article
- MicroRNA-3163 targets ADAM-17 and enhances the sensitivity of hepatocellular carcinoma cells to molecular targeted agents.Cell death & disease · 2019Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Presenilin is the catalytic subunit of γ-secretase, a four-component intramembrane protease responsible for the generation of β-amyloid (Aβ) peptides. Over 200 Alzheimer's disease-related mutations have been identified in presenilin 1 (PS1) and PS2. Here, we report that Bax-inhibitor 1 (BI1), an evolutionarily conserved transmembrane protein, stably associates with PS1. BI1 specifically interacts with PS1 in isolation, but not with PS1 in the context of an assembled γ-secretase. The PS1-BI1 complex exhibits no apparent proteolytic activity, as judged by the inability to produce Aβ40 and Aβ42 from the substrate APP-C99. At an equimolar concentration, BI1 has no impact on the proteolytic activity of γ-secretase; at a 200-fold molar excess, BI1 reduces γ-secretase activity nearly by half. Our biochemical study identified BI1 as a PS1-interacting protein, suggesting additional functions of PS1 beyond its involvement in γ-secretase.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.