Evidence map›Paper›PMID 18243100›Full record

ArticleCell2008

Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signaling.

Melih Acar, Hamed Jafar-Nejad, Hideyuki Takeuchi, Akhila Rajan, Dafina Ibrani, Nadia A Rana, Hongling Pan, Robert S Haltiwanger, Hugo J Bellen

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 167 papers.

0numbers the graph read from it
0cells of the map it votes in
167citing papers in PubMed
10.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

167 citing papers in PubMed, 298 citations in OpenAlex.

  1. Article
  2. Sweet spots of O-glucosylation.Nature chemical biology · 2025
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  4. DifferentialProceedings of the National Academy of Sciences of the United States of America · 2025
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  6. Nagoya journal of medical science · 2025
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  7. The Memory Gene,Biomolecules · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. International journal of molecular sciences · 2024
    Article
  14. Article
  15. Article
  16. Biomolecular NMR assignments · 2023
    Article
  17. Article
  18. Review
  19. Article
  20. Review

107 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Melih AcarProgram in Developmental Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Hamed Jafar-Nejad
Hideyuki Takeuchi
Akhila Rajan
Dafina Ibrani
Nadia A Rana
Hongling Pan
Robert S Haltiwanger
Hugo J Bellen
Baylor College of Medicine · USStony Brook University · USHoward Hughes Medical Institute · US

Funding

UNDERSTANDING FXTAS AMONG MALES WITH THE FMR1 PREMUTATIONP30HD024064 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI TOLIAS, KIMBERLY R · 1988 to 2013
$29.4M
O-Glycosylation of Epidermal Growth Factor-like MotifsR01GM061126 · NIGMS · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S. · 2001 to 2021
$9.1M
Fine-Tuning the Notch Signaling Pathway via O-GlucosylationR01GM084135 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAFAR-NEJAD, HAMED · 2008 to 2017
$2.6M
Howard Hughes Medical InstituteNICHD NIH HHS P30 HD024064NIGMS NIH HHS 5R01GM061126-07NIGMS NIH HHS R01 GM061126NIGMS NIH HHS R01 GM084135PHS HHS T32-GMO7526
6 · The paper itself

Abstract

Notch signaling is broadly used to regulate cell-fate decisions. We have identified a gene, rumi, with a temperature-sensitive Notch phenotype. At 28 degrees C-30 degrees C, rumi clones exhibit a full-blown loss of Notch signaling in all tissues tested. However, at 18 degrees C only a mild Notch phenotype is evident. In vivo analyses reveal that the target of Rumi is the extracellular domain of Notch. Notch accumulates intracellularly and at the cell membrane of rumi cells but fails to be properly cleaved, despite normal binding to Delta. Rumi is an endoplasmic reticulum-retained protein with a highly conserved CAP10 domain. Our studies show that Rumi is a protein O-glucosyltransferase, capable of adding glucose to serine residues in Notch EGF repeats with the consensus C1-X-S-X-P-C2 sequence. These data indicate that by O-glucosylating Notch in the ER, Rumi regulates its folding and/or trafficking and allows signaling at the cell membrane.

Indexed as

Drosophila ProteinsSignal TransductionAllelesAmino Acid SequenceAnimalsChromosome MappingChromosomesConsensus SequenceDrosophilaEmbryo, NonmammalianEndoplasmic ReticulumGene Expression RegulationGenes, InsectGlucoseGlucosyltransferasesGlycosylationDrosophila ProteinsGlucoseGlucosyltransferasesGlycosyltransferasesReceptors, NotchRumi protein, DrosophilaSerine

Identifiers

PMID18243100
PMCPMC2275919
OpenAlexW1967051571

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.