Proteolytic Cleavage Driven by Glycosylation.
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ABSTRACT:
SUBMITTER: Kotzler MP
PROVIDER: S-EPMC4697182 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Publications
Proteolytic Cleavage Driven by Glycosylation.
Kötzler Miriam P MP Withers Stephen G SG
The Journal of biological chemistry 20151029 1
Proteolytic processing of human host cell factor 1 (HCF-1) to its mature form was recently shown, unexpectedly, to occur in a UDP-GlcNAc-dependent fashion within the transferase active site of O-GlcNAc-transferase (OGT) (Lazarus, M. B., Jiang, J., Kapuria, V., Bhuiyan, T., Janetzko, J., Zandberg, W. F., Vocadlo, D. J., Herr, W., and Walker, S. (2013) Science 342, 1235-1239). An interesting mechanism involving formation and then intramolecular rearrangement of a covalent glycosyl ester adduct of ...[more]
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