Polysialic acid on neuropilin-2 is exclusively synthesized by the polysialyltransferase ST8SiaIV and attached to mucintype O-glycans located between the b2 and c domain

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Abstract

Background: Polysialylated neuropilin-2 mediates CCL21-driven chemotactic migration of dendritic cells. Results: Deletion of either ST8SiaIV or O-glycosylation sites located between b2 and c domain abrogates polysialylation of neuropilin-2. Conclusion: Polysialylation of neuropilin-2 occurs in the same linker region as GAGylation of neuropilin-1. Significance: Defining enzyme and acceptor site requirements is crucial for understanding how polysialylation of neuropilin-2 is regulated. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Rollenhagen, M., Buettner, F. F. R., Reismann, M., Jirmo, A. C., Grove, M., Behrens, G. M. N., … Mühlenhoff, M. (2013). Polysialic acid on neuropilin-2 is exclusively synthesized by the polysialyltransferase ST8SiaIV and attached to mucintype O-glycans located between the b2 and c domain. Journal of Biological Chemistry, 288(32), 22880–22892. https://doi.org/10.1074/jbc.M113.463927

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