Evidence map›Paper›PMID 18347015›Full record

ArticleThe Journal of biological chemistry2008

Roles of Pofut1 and O-fucose in mammalian Notch signaling.

Mark Stahl, Kazuhide Uemura, Changhui Ge, Shaolin Shi, Yuko Tashima, Pamela Stanley

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

105 citing papers in PubMed, 174 citations in OpenAlex.

  1. Review
  2. ProteinMolecules (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Notch signaling pathway: architecture, disease, and therapeutics.Signal transduction and targeted therapy · 2022
    Review
  11. O-fucosylation of thrombospondin type 1 repeats is essential for ECM remodeling and signaling during bone development.Matrix biology : journal of the International Society for Matrix Biology · 2022
    Article
  12. Review
  13. Signaling at Physical Barriers during Pollen-Pistil Interactions.International journal of molecular sciences · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Pleiotropic Role of Notch Signaling in Human Skin Diseases.International journal of molecular sciences · 2020
    Review
  20. Article

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

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Mark StahlDepartment of Cell Biology, Albert Einstein College of Medicine, New York, New York 10461, USA.
Kazuhide Uemura
Changhui Ge
Shaolin Shi
Yuko Tashima
Pamela Stanley
Albert Einstein College of Medicine · USYeshiva University · USIcahn School of Medicine at Mount Sinai · USUniversity of Shizuoka · JP

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007288 · NIGMS · YESHIVA UNIVERSITY · PI AKABAS, MYLES H. · 1985 to 2022
$35.6M
Roles of Glycoslyation in Notch SignalingR01CA095022 · NCI · YESHIVA UNIVERSITY · PI STANLEY, PAMELA M · 2002 to 2011
$4.1M
NCI NIH HHS CA 95022NIGMS NIH HHS T32 GM07288PHS HHS P01 13330
6 · The paper itself

Abstract

Mammalian Notch receptors contain 29-36 epidermal growth factor (EGF)-like repeats that may be modified by protein O-fucosyltransferase 1 (Pofut1), an essential component of the canonical Notch signaling pathway. The Drosophila orthologue Ofut1 is proposed to function as both a chaperone required for stable cell surface expression of Notch and a protein O-fucosyltransferase. Here we investigate these dual roles of Pofut1 in relation to endogenous Notch receptors of Chinese hamster ovary and murine embryonic stem (ES) cells. We show that fucosylation-deficient Lec13 Chinese hamster ovary cells have wild type levels of Pofut1 and cell surface Notch receptors. Nevertheless, they have reduced binding of Notch ligands and low levels of Delta1- and Jagged1-induced Notch signaling. Exogenous fucose but not galactose rescues both ligand binding and Notch signaling. Murine ES cells lacking Pofut1 also have wild type levels of cell surface Notch receptors. However, Pofut1-/- ES cells do not bind Notch ligands or exhibit Notch signaling. Although overexpression of fucosyltransferase-defective Pofut1 R245A in Pofut1-/- cells partially rescues ligand binding and Notch signaling, this effect is not specific. The same rescue is achieved by an unrelated, inactive, endoplasmic reticulum glucosidase. Therefore, mammalian Notch receptors require Pofut1 for the generation of optimally functional Notch receptors, but, in contrast to Drosophila, Pofut1 is not required for stable cell surface expression of Notch. Importantly, we also show that, under certain circumstances, mammalian Notch receptors are capable of signaling in the absence of Pofut1 and O-fucose.

Indexed as

AnimalsCell LineCell MembraneCHO CellsCricetinaeCricetulusEndoplasmic ReticulumFucoseFucosyltransferasesHumansMiceMice, TransgenicModels, BiologicalReceptors, NotchSignal TransductionFucoseFucosyltransferasespolypeptide fucosyltransferaseReceptors, Notch

Identifiers

PMID18347015
PMCPMC2376238
OpenAlexW2047582243

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.