2012 Fiscal Year Final Research Report
Biological and biochemical analyses of Drosophilamutants lacking a novel O-GlcNAc modification
| Project/Area Number |
23790328
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
General medical chemistry
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| Research Institution | Nagoya University |
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Principal Investigator |
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| Project Period (FY) |
2011 – 2012
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| Keywords | Notch受容体 / 糖鎖修飾 / O-結合型糖鎖 / O-GlcNAc転移酵素 |
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| Research Abstract |
The O-linked- N -acetylglucosamine (O-GlcNAc) modifi cation of cytoplasmic and nuclear proteins regulates basic cellular functions and is involved in the aetiology of diabetes and neurodegeneration. This intracellular O-GlcNAcylation is catalyzed by a single O-GlcNAc transferase, OGT. Here we report a novel OGT, EOGT, responsible for extracellular O-GlcNAcylation. Although both OGT and EOGT are regulated by hexosamine fl ux, EOGT localizes to the lumen of the endoplasmic reticulum and transfers GlcNAc to epidermal growth factor-like domains in an OGT-independent manner. Loss of Eogt gives phenotypes similar to those caused by defects in the apical extracellular matrix. Dumpy, a membrane-anchored extracellular protein, is O-GlcNAcylated, and EOGT is required for Dp-dependent epithelial cell - matrix interactions. Thus, O-GlcNAcylation of secreted and membrane glycoproteins is a novel mediator of cell - cell or cell - matrix interactions at the cell surface.
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[Journal Article] pp-GalNAc-T13 induces high metastatic potential of murine Lewis lung cancer by generating trimeric Tn antigen2012
Author(s)
Matsumoto Y, Zhang Q, Akita K, Nakada H, Hamamura K, Tokuda N, Tsuchida A, Matsubara T, Hori T, Okajima T, Furukawa K, Urano T, Furukawa K
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Journal Title
Biochem Biophys Res Commun
Volume: 419
Pages: 7-13
Peer Reviewed
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