ArticleThe Journal of biological chemistry2010
Structure and mutagenesis of neural cell adhesion molecule domains: evidence for flexibility in the placement of polysialic acid attachment sites.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- In planta engineering of polysialylated glycoproteins using salmonid polysialyltransferases.Scientific reports · 2026Article
- Engineering Peptide Modulators for T-Cell Migration by Structural Scaffold Matching.Journal of medicinal chemistry · 2025Article
- The Polybasic Region of the Polysialyltransferase ST8Sia-IV Binds Directly to the Neural Cell Adhesion Molecule, NCAM.Biochemistry · 2017Article
- Sialylation of N-glycans: mechanism, cellular compartmentalization and function.Histochemistry and cell biology · 2017Review
- Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation.Nature structural & molecular biology · 2015Article
- Protein glycosylation in cancer.Annual review of pathology · 2015Review
- Characterisation of genetic variation in ST8SIA2 and its interaction region in NCAM1 in patients with bipolar disorder.PloS one · 2014Article
- Identification of potential glycan cancer markers with sialic acid attached to sialic acid and up-regulated fucosylated galactose structures in epidermal growth factor receptor secreted from A431 cell line.Molecular & cellular proteomics : MCP · 2013Article
- The polysialyltransferases interact with sequences in two domains of the neural cell adhesion molecule to allow its polysialylation.The Journal of biological chemistry · 2013Article
- Sequences prior to conserved catalytic motifs of polysialyltransferase ST8Sia IV are required for substrate recognition.The Journal of biological chemistry · 2012Article
- Two group A streptococcal peptide pheromones act through opposing Rgg regulators to control biofilm development.PLoS pathogens · 2011Article
- Site-specific enzymatic polysialylation of therapeutic proteins using bacterial enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Sequences at the interface of the fifth immunoglobulin domain and first fibronectin type III repeat of the neural cell adhesion molecule are critical for its polysialylation.The Journal of biological chemistry · 2011Article
- Sequences from the first fibronectin type III repeat of the neural cell adhesion molecule allow O-glycan polysialylation of an adhesion molecule chimera.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The addition of alpha2,8-polysialic acid to the N-glycans of the neural cell adhesion molecule, NCAM, is critical for brain development and plays roles in synaptic plasticity, learning and memory, neuronal regeneration, and the growth and invasiveness of cancer cells. Our previous work indicates that the polysialylation of two N-glycans located on the fifth immunoglobulin domain (Ig5) of NCAM requires the presence of specific sequences in the adjacent fibronectin type III repeat (FN1). To understand the relationship of these two domains, we have solved the crystal structure of the NCAM Ig5-FN1 tandem. Unexpectedly, the structure reveals that the sites of Ig5 polysialylation are on the opposite face from the FN1 residues previously found to be critical for N-glycan polysialylation, suggesting that the Ig5-FN1 domain relationship may be flexible and/or that there is flexibility in the placement of Ig5 glycosylation sites for polysialylation. To test the latter possibility, new Ig5 glycosylation sites were engineered and their polysialylation tested. We observed some flexibility in glycosylation site location for polysialylation and demonstrate that the lack of polysialylation of a glycan attached to Asn-423 may be in part related to a lack of terminal processing. The data also suggest that, although the polysialyltransferases do not require the Ig5 domain for NCAM recognition, their ability to engage with this domain is necessary for polysialylation to occur on Ig5 N-glycans.
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