ArticlePLoS genetics2014
The protein O-glucosyltransferase Rumi modifies eyes shut to promote rhabdomere separation in Drosophila.
Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 34 citations in OpenAlex.
- ER quality control of Crumbs2 and Notch proteins by GXYLT1-dependent xylosyl elongation of O-glucose glycans.The Journal of biological chemistry · 2026Article
- The glycosyltransferase POGLUT1 regulates muscle stem cell development and maintenance in mice.PLoS genetics · 2025Article
- The role of m5C, m1A and m7G modifications in tumors of urinary system.Frontiers in cell and developmental biology · 2025Review
- The glycosyltransferase POGLUT1 regulates muscle stem cell development and maintenance in mice.bioRxiv : the preprint server for biology · 2024Article
- Phototoxicity avoidance is a potential therapeutic approach for retinal dystrophy caused by EYS dysfunction.JCI insight · 2024Article
- Disease modeling and gene correction of LGMDR21 iPSCs elucidates the role of POGLUT1 in skeletal muscle maintenance, regeneration, and the satellite cell niche.Molecular therapy. Nucleic acids · 2023Article
- Dissecting the role of EYS in retinal degeneration: clinical and molecular aspects and its implications for future therapy.Orphanet journal of rare diseases · 2021Review
- Structure, function, and pathology of protein O-glucosyltransferases.Cell death & disease · 2021Review
- Multifaceted regulation of Notch signaling by glycosylation.Glycobiology · 2021Review
- Other Types of Glycosylation.Advances in experimental medicine and biology · 2021Article
- Extracellular matrix dynamics in tubulogenesis.Cellular signalling · 2020Review
- A Chemoenzymatic Method Based on Easily Accessible Enzymes for Profiling Protein O-GlcNAcylation.Analytical chemistry · 2020Article
- Synthesis and biological roles of O-glycans in insects.Glycoconjugate journal · 2020Review
- O-Linked glycosylation in Drosophila melanogaster.Current opinion in structural biology · 2019Review
- Sensitized genetic backgrounds reveal differential roles for EGF repeat xylosyltransferases in Drosophila Notch signaling.Glycobiology · 2018Article
- Congenital diseases caused by defectiveNagoya journal of medical science · 2018Review
- A dual role of the extracellular domain ofBiology open · 2018Article
- Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1).Nature communications · 2017Article
- Ablation of EYS in zebrafish causes mislocalisation of outer segment proteins, F-actin disruption and cone-rod dystrophy.Scientific reports · 2017Article
- The Crumbs_C isoform ofBiology open · 2017Article
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 at 3 institutions in 1 country.
Funding
Abstract
The protein O-glucosyltransferase Rumi/POGLUT1 regulates Drosophila Notch signaling by adding O-glucose residues to the Notch extracellular domain. Rumi has other predicted targets including Crumbs (Crb) and Eyes shut (Eys), both of which are involved in photoreceptor development. However, whether Rumi is required for the function of Crb and Eys remains unknown. Here we report that in the absence of Rumi or its enzymatic activity, several rhabdomeres in each ommatidium fail to separate from one another in a Notch-independent manner. Mass spectral analysis indicates the presence of O-glucose on Crb and Eys. However, mutating all O-glucosylation sites in a crb knock-in allele does not cause rhabdomere attachment, ruling out Crb as a biologically-relevant Rumi target in this process. In contrast, eys and rumi exhibit a dosage-sensitive genetic interaction. In addition, although in wild-type ommatidia most of the Eys protein is found in the inter-rhabdomeral space (IRS), in rumi mutants a significant fraction of Eys remains in the photoreceptor cells. The intracellular accumulation of Eys and the IRS defect worsen in rumi mutants raised at a higher temperature, and are accompanied by a ∼50% decrease in the total level of Eys. Moreover, removing one copy of an endoplasmic reticulum chaperone enhances the rhabdomere attachment in rumi mutant animals. Altogether, our data suggest that O-glucosylation of Eys by Rumi ensures rhabdomere separation by promoting proper Eys folding and stability in a critical time window during the mid-pupal stage. Human EYS, which is mutated in patients with autosomal recessive retinitis pigmentosa, also harbors multiple Rumi target sites. Therefore, the role of O-glucose in regulating Eys may be conserved.
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.