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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Glucosamine- induced insulin resistance is coupled to O- linked glycosylation of Munc18c.

Evidence suggests that glucosamine inhibits distal components regulating insulin-stimulated GLUT4 translocation to the plasma membrane. Here we assessed whether key membrane docking and fusion events were targeted. Consistent with a plasma membrane-localized effect, 3T3-L1 adipocytes exposed to glucosamine displayed an increase in cell-surface O-linked glycosylation and a simultaneously impaired mobilization of GLUT4 by insulin. Analysis of syntaxin 4 and SNAP23, plasma membrane-localized target receptor proteins (t-SNAREs) for the GLUT4 vesicle, showed that they were not cell-surface targets of O-linked glycosylation. However, the syntaxin 4 binding protein, Munc18c, was targeted by O-linked glycosylation. This occurred concomitantly with a block in insulin-stimulated association of syntaxin 4 with its cognate GLUT4 vesicle receptor protein (v-SNARE), VAMP2. In conclusion, our data suggest that the mechanism by which glucosamine inhibits insulin- stimulated GLUT4 translocation involves modification of Munc18c.[1]


  1. Glucosamine-induced insulin resistance is coupled to O-linked glycosylation of Munc18c. Chen, G., Liu, P., Thurmond, D.C., Elmendorf, J.S. FEBS Lett. (2003) [Pubmed]
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