Trends in Glycoscience and Glycotechnology
Online ISSN : 1883-2113
Print ISSN : 0915-7352
ISSN-L : 0915-7352
Volume 20, Issue 113
Displaying 1-5 of 5 articles from this issue
  • Hideyuki Takeuchi, Haltiwanger Robert S.
    2008 Volume 20 Issue 113 Pages 159-170
    Published: 2008
    Released on J-STAGE: November 20, 2008
    Notch signaling regulates numerous cell fate decisions during development. In a genetic screen designed to isolate new components of this pathway, mutations in a novel gene, rumi, were identified to cause a temperature-sensitive phenotype. At 28-30°C, rumi clones exhibited a full-blown Notch phenotype in all the examined tissues. However, at 18°C, only a mild Notch phenotype was evident. Notch accumulated intracellularly and in the cell membrane of rumi cells, but was not properly processed despite normal binding to Delta. Rumi is an endoplasmic reticulum (ER)-retained protein with a highly conserved CAP10 domain. Our studies showed that Rumi is a protein O-glucosyltransferase (Poglut), capable of adding glucose in an O-linkage to serine residues in the consensus C1-X-S-X-P-C2 sequence within the EGF repeats of the Notch extracellular domain. These data indicate that Rumi regulates Notch folding and/or trafficking and allows signaling at the cell membrane by O-glucosylation of Notch in the ER. Here, we, in collaboration with Dr. Hugo Bellen's laboratory, describe our method of discovery of Rumi (1). We also highlight the functional importance of O-linked sugar modifications on Notch.
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