Glucosylation of Pre-Notch by Poglut1

Stable Identifier
R-MMU-2023179
Type
Reaction [transition]
Species
Mus musculus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Glucosylation of Pre-Notch by Poglut1
In addition to fucosylation of Notch receptor precursors, glucosylation is another crucial step in Notch processing, required for the receptor to be fully functional. Endoplasmic reticulum O-glucosyl transferase Poglut1, homolog of Drosophila Rumi, adds a glucosyl group to conserved serine residues within EGF repeats of Notch. The consensus sequence of Poglut1 glucosylation sites is C1-X-S-X-P-C2, where C1 and C2 are the first and second cysteine residue in the EGF repeat, respectively, while X represents any amino acid. Only those glucosylation sites that are conserved between human, mouse and rat isoforms are shown.
Literature References
PubMed ID Title Journal Year
21490058 Regulation of mammalian Notch signaling and embryonic development by the protein O-glucosyltransferase Rumi

Lopez, M, Fernandez-Valdivia, R, Takeuchi, H, Leonardi, J, Haltiwanger, RS, Jafar-Nejad, H, Samarghandi, A

Development 2011
18243100 Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signaling

Rajan, A, Pan, H, Takeuchi, H, Acar, M, Rana, NA, Haltiwanger, RS, Bellen, HJ, Jafar-Nejad, H, Ibrani, D

Cell 2008
Participants
Catalyst Activity

UDP-glucosyltransferase activity of Poglut1 [endoplasmic reticulum lumen]

Orthologous Events
Authored
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