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Glycobiology Advance Access originally published online on July 1, 2009
Glycobiology 2009 19(10):1068-1077; doi:10.1093/glycob/cwp092
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Effects of N-glycosylation on the activity and localization of GlcNAc-6-sulfotransferase 1

Marguerite M Desko2, David A Gross2 and Jennifer J Kohler1,3

2 Department of Chemistry, Stanford University, Stanford, CA 94305
3 Division of Translational Research, Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA

1 To whom correspondence should be addressed: Tel: +214-648-1214; Fax: +214-648-4156; e-mail: Jennifer.Kohler{at}UTSouthwestern.edu

Received on May 20, 2009; revised on June 17, 2009; accepted on June 17, 2009

N-Acetylglucosamine-6-sulfotransferase-1 (GlcNAc6ST-1) is a Golgi-resident glycoprotein that is responsible for sulfation of the L-selectin ligand on endothelial cells. Here, we report the sites at which GlcNAc6ST-1 is modified with N-linked glycans and the effects that each glycan has on enzyme activity, specificity, and localization. We determined that glycans are added at three of four potential N-linked glycosylation sites: N196, N410, and N428. The N428 glycan is required for the production of sulfated cell surface glycans: cells expressing a mutant enzyme lacking this glycan were unable to sulfate the sialyl Lewis X tetrasaccharide or a putative extended core 1 O-linked glycan. The N196 and N410 glycans differentially affect sulfation of two different substrates: cells that express an enzyme lacking the N410 glycan are able to sulfate the sialyl Lewis X substrate, but produce reduced levels of a sulfated peripheral lymph node addressin epitope and cells that express an enzyme lacking the N196 glycan are able to produce a sulfated peripheral lymph node addressin epitope, but are impaired in their ability to sulfate sialyl Lewis X. The glycans’ effects on enzyme activity may be mediated, in part, by changes in enzyme localization. While most mutants that lacked glycans localized normally within the Golgi, the N428A mutant and a mutant lacking all glycans were also found to localize ectopically. Altered trafficking of mutants may be associated with the mechanisms by which misglycosylated enzyme is degraded.

Key words: enzyme specificity / N-linked glycosylation / sulfation


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