ArticlebioRxiv : the preprint server for biology2026
VPS4 and CHMP7 release centromeres from the nuclear envelope for post-mitotic positioning in daughter nuclei.
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Eukaryotic chromosomes occupy ordered configurations within the nucleus, an organization that must be re-established in daughter cells as the nuclear envelope reforms at the end of mitosis. The conserved enzyme VPS4 and ESCRT-III proteins mediate nuclear envelope reformation, yet their role in post-mitotic centromere positioning remains unclear. Here, we develop a chemical genetics approach to analyze the role of VPS4 in human cells. VPS4 inhibition prevents the clearance of CHMP7 from centromeres, which remain constrained in ring-like configurations established during mitosis. Without VPS4 activity, CHMP7, but not other ESCRT-III proteins, forms nuclear foci, nuclear envelope protein distribution is altered and inner nuclear membrane invaginations appear. Following these defects, DNA damage is observed in the vicinity of centromeres. Depletion of CHMP7, but not CHMP4B, suppresses this damage. We propose that VPS4-mediated turnover of CHMP7 releases centromeres from transient nuclear envelope contacts, ensuring their proper positioning after mitosis and maintaining genome integrity.
Identifiers
What Socratic 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 Socratic graph.