ArticleCell death discovery2025
Nesprin-2 contains BH3-like motifs that can promote cell death.
Article in Cell death discovery, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Direct binding of the C-terminal sequences of Bim and Bak contributes to efficient Bak activation.Cell death and differentiation · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
BH3-only proteins are a subgroup of the pro-apoptotic Bcl-2 family proteins. They initiate apoptosis by interacting with the multidomain pro- and anti-apoptotic Bcl-2 family proteins. SYNE2 encodes multiple nesprin-2 (Nes2) isoforms of which the most abundant and the largest is the nuclear envelope protein nesprin-2 giant (Nes2G). Nes2G is a component of the nuclear envelope Linker of Nucleoskeleton and Cytoskeleton (LINC) complex that connects the nucleus and the cytoskeleton. Previously, we showed that Nes2 has pro-apoptotic activity. We now show that Nes2G can bind multidomain pro-apoptotic and anti-apoptotic Bcl-2 family proteins and contains two BH3-like motifs near its N- and C-termini. Molecular modeling predicts that these BH3-like motifs have amphipathic α-helix structures and can dock onto the canonical groove of Bax and anti-apoptotic proteins as well as the trigger site of Bax. A chimeric tBid with its BH3 domain replaced with the C-terminal Nes2 BH3-like domain binds to Bax in cells. Furthermore, Nes2 BH3-like motif-containing fragments from the N- and the C-termini bind both pro-apoptotic and anti-apoptotic Bcl-2 proteins and promote cytochrome c release (indicative of apoptosis). Our results suggest that Nes2 acts as a BH3-only protein that regulates apoptosis by binding to the multidomain Bcl-2 family proteins.
Identifiers
What OpenQuestion holds
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.