ArticleThe Journal of biological chemistry2013
Polysialic acid on neuropilin-2 is exclusively synthesized by the polysialyltransferase ST8SiaIV and attached to mucin-type o-glycans located between the b2 and c domain.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 43 citations in OpenAlex.
- Polysialic acid is associated with immune activation in human peripheral blood nuclear cells.Glycobiology · 2026Article
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- Polysialylation controls immune function of myeloid cells in murine model of pneumococcal pneumonia.Cell reports · 2023Article
- Neuroimmunomodulatory properties of polysialic acid.Glycoconjugate journal · 2023Review
- Comprehensive Analysis of Oligo/Polysialylglycoconjugates in Cancer Cell Lines.International journal of molecular sciences · 2022Article
- News and Views on Polysialic Acid: From Tumor Progression and Brain Development to Psychiatric Disorders, Neurodegeneration, Myelin Repair and Immunomodulation.Frontiers in cell and developmental biology · 2022Review
- Polysialic Acid in the Immune System.Frontiers in immunology · 2021Review
- Autopolysialylation of polysialyltransferases is required for polysialylation and polysialic acid chain elongation on select glycoprotein substrates.The Journal of biological chemistry · 2018Article
- Multiple Roles of Glycans in Hematological Malignancies.Frontiers in oncology · 2018Review
- Sialylation of N-glycans: mechanism, cellular compartmentalization and function.Histochemistry and cell biology · 2017Review
- Multifaceted Role of Neuropilins in the Immune System: Potential Targets for Immunotherapy.Frontiers in immunology · 2017Review
- Review
- Class 3 semaphorins induce F-actin reorganization in human dendritic cells: Role in cell migration.Journal of leukocyte biology · 2016Article
- Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study.Journal of visualized experiments : JoVE · 2016Article
- Structural studies of neuropilin-2 reveal a zinc ion binding site remote from the vascular endothelial growth factor binding pocket.The FEBS journal · 2016Article
- Sequence Requirements for Neuropilin-2 Recognition by ST8SiaIV and Polysialylation of Its O-Glycans.The Journal of biological chemistry · 2016Article
- Polysialylation controls dendritic cell trafficking by regulating chemokine recognition.Science (New York, N.Y.) · 2016Article
- Molecular characterization and expression analyses of ST8Sia II and IV in piglets during postnatal development: lack of correlation between transcription and posttranslational levels.Glycoconjugate journal · 2015Article
- Protein glycosylation in cancer.Annual review of pathology · 2015Review
- Changes in polysialic acid expression on myeloid cells during differentiation and recruitment to sites of inflammation: role in phagocytosis.Glycobiology · 2014Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neuropilin-2 (NRP2) is well known as a co-receptor for class 3 semaphorins and vascular endothelial growth factors, involved in axon guidance and angiogenesis. Moreover, NRP2 was shown to promote chemotactic migration of human monocyte-derived dendritic cells (DCs) toward the chemokine CCL21, a function that relies on the presence of polysialic acid (polySia). In vertebrates, this posttranslational modification is predominantly found on the neural cell adhesion molecule (NCAM), where it is synthesized on N-glycans by either of the two polysialyltransferases, ST8SiaII or ST8SiaIV. In contrast to NCAM, little is known on the biosynthesis of polySia on NRP2. Here we identified the polySia attachment sites and demonstrate that NRP2 is recognized only by ST8SiaIV. Although polySia-NRP2 was found on bone marrow-derived DCs from wild-type and St8sia2(-/-) mice, polySia was completely lost in DCs from St8sia4(-/-) mice despite normal NRP2 expression. In COS-7 cells, co-expression of NRP2 with ST8SiaIV but not ST8SiaII resulted in the formation of polySia-NRP2, highlighting distinct acceptor specificities of the two polysialyltransferases. Notably, ST8SiaIV synthesized polySia selectively on a NRP2 glycoform that was characterized by the presence of sialylated core 1 and core 2 O-glycans. Based on a comprehensive site-directed mutagenesis study, we localized the polySia attachment sites to an O-glycan cluster located in the linker region between b2 and c domain. Combined alanine exchange of Thr-607, -613, -614, -615, -619, and -624 efficiently blocked polysialylation. Restoration of single sites only partially rescued polysialylation, suggesting that within this cluster, polySia is attached to more than one site.
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