ArticleJournal of experimental botany2025
ECLIPSE mediates selective degradation of inner nuclear membrane protein in plants.
Article in Journal of experimental botany, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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
3 citing papers in PubMed.
- A multiomics atlas of theScience advances · 2026Article
- Plant UBX domain-containing proteins use distinct strategies to stably engage the unfoldase CDC48A.Plant & cell physiology · 2026Article
- Plant proteases: guardians of proteome integrity and regulators of protein function.Journal of experimental botany · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The inner nuclear membrane (INM) hosts a unique set of membrane proteins essential for nuclear functions. Proteolytic removal of mislocalized or defective membrane proteins is of critical importance for maintaining the homeostasis and integrity of the INM. Previous studies revealed that INM protein degradation depends on a specialized ubiquitin-proteasome system termed INM-associated degradation (INMAD) in plants, requiring the CDC48 complex and the 26S proteasome for membrane protein retrotranslocation and destruction, respectively. However, details of the adaptor proteins that link membrane substrates to the CDC48/proteasome degradation machinery are still lacking in the pathway. Here, we report the discovery of ECLIPSE, a previously uncharacterized protein that may serve as such a molecular bridge in the degradation of the conserved INM protein SUN1. We demonstrate that ECLIPSE physically associates with CDC48 and exhibits strong transcriptional co-regulation with multiple established plant INMAD components. Mechanistically, ECLIPSE may act as an adaptor through its dual-domain architecture: its C-terminal PUB domain mediates direct interaction with CDC48, while its N-terminal ubiquitin-associated domain recognizes ubiquitinated INM substrates. Genetic and biochemical analyses further established that ECLIPSE is required for SUN1 protein degradation in Arabidopsis, supporting its role in the turnover of at least some INM proteins in plants.
Indexed as
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.