Journal
CELL
Volume 132, Issue 2, Pages 247-258Publisher
CELL PRESS
DOI: 10.1016/j.cell.2007.12.016
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NICHD NIH HHS [P30 HD024064] Funding Source: Medline
- NIGMS NIH HHS [R01 GM084135-01, R01 GM061126, 5R01GM061126-07, R01 GM084135] Funding Source: Medline
- PHS HHS [T32-GMO7526] Funding Source: Medline
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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 C-1-X-S-X-P-C-2 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.
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