2008
DOI: 10.1074/jbc.m806202200
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O-Linked N-Acetylglucosamine Is Present on the Extracellular Domain of Notch Receptors

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Cited by 155 publications
(158 citation statements)
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“…We also identified an O-GlcNAc site on the EGF-like domain of NOTCH2 protein of the Notch signaling pathway, which we infer is on the T residue in the YSCVCSPGFTGQR sequence, consistent with the CXXGXS/ TGXXC motif (Table 3). Our findings suggest that this EOGT (36) has additional substrates. In fact, we determined that 91 mouse proteins, 104 human proteins, and 18 Drosophila proteins contain the CXXGXS/TGXXC motif (Datasets S6, S7, and S8).…”
Section: O-glcnacylation On a Secreted Protein And On The Extracellularmentioning
confidence: 55%
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“…We also identified an O-GlcNAc site on the EGF-like domain of NOTCH2 protein of the Notch signaling pathway, which we infer is on the T residue in the YSCVCSPGFTGQR sequence, consistent with the CXXGXS/ TGXXC motif (Table 3). Our findings suggest that this EOGT (36) has additional substrates. In fact, we determined that 91 mouse proteins, 104 human proteins, and 18 Drosophila proteins contain the CXXGXS/TGXXC motif (Datasets S6, S7, and S8).…”
Section: O-glcnacylation On a Secreted Protein And On The Extracellularmentioning
confidence: 55%
“…The O-GlcNAc transferase that attaches O-β-GlcNAc to NOTCH is a distinct enzyme that is genetically unrelated to OGT (36). It resides in the endoplasmic reticulum (ER) within the secretory pathway and is termed EGF domain-specific O-GlcNAc transferase (EOGT) (36,37).…”
Section: O-glcnacylation On a Secreted Protein And On The Extracellularmentioning
confidence: 99%
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“…The EGF-like repeats in the extracellular domain of Notch and other vertebrate proteins are modified by O-fucose and O-glucose glycans (Rampal et al 2007;Stanley and Okajima 2010), as well as O-GlcNAc (Matsuura et al 2008; Fig. 1).…”
Section: O-glycosylationmentioning
confidence: 99%