Both N- and O-linked glycans have been implicated as apical targeting signals. We seek to understand how these posttranslational modifications are recognized and enable segregation of selected membrane and secretory proteins into apically-destined vesicles. We have found that apical sorting of the sialomucin endolyn is dependent on terminal processing of two of the eight N-glycans on the protein. We are currently working to dissect the molecular mechanism(s) that directs polarized sorting of endolyn along both the biosynthetic and postendocytic pathways.
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