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Publication : Plakoglobin is O-glycosylated close to the N-terminal destruction box.

First Author  Hatsell S Year  2003
Journal  J Biol Chem Volume  278
Issue  39 Pages  37745-52
PubMed ID  12847106 Mgi Jnum  J:85670
Mgi Id  MGI:2675927 Doi  10.1074/jbc.M301346200
Citation  Hatsell S, et al. (2003) Plakoglobin is O-glycosylated close to the N-terminal destruction box. J Biol Chem 278(39):37745-52
abstractText  Plakoglobin provides a key linkage in protein chains that connect desmosomal and classical cadherins to the cytoskeleton. It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin. The closely related protein, beta-catenin, is rapidly targeted for proteasomal degradation by phosphorylation of a 'destruction box' within the N-terminal domain. Inhibition of this process forms the basis of Wnt signaling. This destruction box is also found in the N-terminal domain of plakoglobin. We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box. O-GlcNAc modification has been proposed to counteract phosphorylation, provide protection from proteasomal degradation, mediate signal transduction, silence transcription, and regulate multimolecular protein assembly. This finding has potential implications for understanding the roles of plakoglobin.
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