ReviewTrends in plant science2025
Uvr motifs regulate the chloroplast Clp chaperone-protease system.
Review in Trends in plant science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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.
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Who cites it
2 citing papers in PubMed.
- EXECUTER-mediated singlet oxygen signaling in plants: Mechanisms, evolution, and functional diversification.Plant communications · 2026Review
- The schizophrenia associated protein DISC1 forms a multivalent tetrameric hub via conserved UVR dimers.Nature communications · 2026Article
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Authors and funding
3 authors.
Funding
Abstract
Chloroplast proteostasis relies on diverse proteases, including the essential Clp chaperone-protease system. Two chloroplast ClpC AAA+ chaperones and the plant-specific adaptor ClpF contain an Uvr motif with predicted coiled-coiled structures implicated in protein-protein interactions. Head-to-head contacts between Uvr motifs in middle (M)-domains regulate the oligomerization and activation of several bacterial Clp chaperones. Interestingly, in arabidopsis (Arabidopsis thaliana), this Uvr motif is found in six additional chloroplast proteins (Executer1, Executer2, and Uvr1-4). Here, we first summarize evidence that Uvr motifs regulate proteostasis in bacteria. Based on this evidence and recent results in arabidopsis, we postulate that arabidopsis Uvr motif proteins regulate chloroplast Clp proteolysis. We propose specific working hypotheses to test the function of the Uvr motif in chloroplast proteostasis.
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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.