ArticleThe Journal of biological chemistry2010
N-glycosylation at the SynCAM (synaptic cell adhesion molecule) immunoglobulin interface modulates synaptic adhesion.
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 40 papers.
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Who cites it
40 citing papers in PubMed, 64 citations in OpenAlex.
- Understanding protein ISGylation, a multifaceted posttranslational modification.Cell chemical biology · 2026Review
- SynCAMs in Normal Vertebrate Neural Development and Neuropsychiatric Disorders: from the Perspective of the OCAs.Molecular neurobiology · 2024Review
- Advances in post-translational modifications of proteins and cancer immunotherapy.Frontiers in immunology · 2023Review
- Mathematical model of mechanobiology of acute and repeated synaptic injury and systemic biomarker kinetics.Frontiers in cellular neuroscience · 2023Article
- Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning.EMBO reports · 2022Article
- Identification of substrates of palmitoyl protein thioesterase 1 highlights roles of depalmitoylation in disulfide bond formation and synaptic function.PLoS biology · 2022Article
- Tissue specific expression of sialic acid metabolic pathway: role in GNE myopathy.Journal of muscle research and cell motility · 2021Article
- Differential Contribution of Cadm1-Cadm3 Cell Adhesion Molecules to Peripheral Myelinated Axons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Polysialic Acid in the Immune System.Frontiers in immunology · 2021Review
- Synaptic recognition molecules in development and disease.Current topics in developmental biology · 2021Article
- Molecular Mechanisms of L1 and NCAM Adhesion Molecules in Synaptic Pruning, Plasticity, and Stabilization.Frontiers in cell and developmental biology · 2021Review
- Brain region-dependent alterations in polysialic acid immunoreactivity across the estrous cycle in mice.Hormones and behavior · 2020Article
- Adhesion Protein Structure, Molecular Affinities, and Principles of Cell-Cell Recognition.Cell · 2020Review
- Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Latrophilin's Social Protein Network.Frontiers in neuroscience · 2019Review
- Immunoglobulin-Like Receptors and Their Impact on Wiring of Brain Synapses.Annual review of genetics · 2018Review
- Cell adhesion molecule-1 shedding induces apoptosis of renal epithelial cells and exacerbates human nephropathies.American journal of physiology. Renal physiology · 2018Article
- Quantitative Analysis of Interaction Between CADM1 and Its Binding Cell-Surface Proteins Using Surface Plasmon Resonance Imaging.Frontiers in cell and developmental biology · 2018Article
- Modest Static Pressure Can Cause Enteric Nerve Degeneration Through Ectodomain Shedding of Cell Adhesion Molecule 1.Molecular neurobiology · 2017Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Select adhesion molecules connect pre- and postsynaptic membranes and organize developing synapses. The regulation of these trans-synaptic interactions is an important neurobiological question. We have previously shown that the synaptic cell adhesion molecules (SynCAMs) 1 and 2 engage in homo- and heterophilic interactions and bridge the synaptic cleft to induce presynaptic terminals. Here, we demonstrate that site-specific N-glycosylation impacts the structure and function of adhesive SynCAM interactions. Through crystallographic analysis of SynCAM 2, we identified within the adhesive interface of its Ig1 domain an N-glycan on residue Asn(60). Structural modeling of the corresponding SynCAM 1 Ig1 domain indicates that its glycosylation sites Asn(70)/Asn(104) flank the binding interface of this domain. Mass spectrometric and mutational studies confirm and characterize the modification of these three sites. These site-specific N-glycans affect SynCAM adhesion yet act in a differential manner. Although glycosylation of SynCAM 2 at Asn(60) reduces adhesion, N-glycans at Asn(70)/Asn(104) of SynCAM 1 increase its interactions. The modification of SynCAM 1 with sialic acids contributes to the glycan-dependent strengthening of its binding. Functionally, N-glycosylation promotes the trans-synaptic interactions of SynCAM 1 and is required for synapse induction. These results demonstrate that N-glycosylation of SynCAM proteins differentially affects their binding interface and implicate post-translational modification as a mechanism to regulate trans-synaptic adhesion.
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