Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning Rahman, Maisha Ramirez, Nelson Diaz‐Balzac, Carlos A Bülow, Hannes E Genetics Molecular Biology Biochemistry ddc:570 N-glycans are molecularly diverse sugars borne by over 70% of proteins transiting the secretory pathway and have been implicated in protein folding, stability, and localization. Mutations in genes important for N-glycosylation result in congenital disorders of glycosylation that are often associated with intellectual disability. Here, we show that structurally distinct N-glycans regulate an extracellular protein complex involved in the patterning of somatosensory dendrites in Caenorhabditis elegans. Specifically, aman-2/Golgi alpha-mannosidase II, a conserved key enzyme in the biosynthesis of specific N-glycans, regulates the activity of the Menorin adhesion complex without obviously affecting the protein stability and localization of its components. AMAN-2 functions cell-autonomously to allow for decoration of the neuronal transmembrane receptor DMA-1/LRR-TM with the correct set of high-mannose/hybrid/paucimannose N-glycans. Moreover, distinct types of N-glycans on specific N-glycosylation sites regulate DMA-1/LRR-TM receptor function, which, together with three other extracellular proteins, forms the Menorin adhesion complex. In summary, specific N-glycan structures regulate dendrite patterning by coordinating the activity of an extracellular adhesion complex, suggesting that the molecular diversity of N-glycans can contribute to developmental specificity in the nervous system. Embo Press 2022 info:eu-repo/semantics/article doc-type:Article Article http://purl.org/coar/resource_type/c_2df8fbb1 https://research-explorer.ista.ac.at/record/12275 Rahman M, Ramirez N, Diaz‐Balzac CA, Bülow HE. Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning. <i>EMBO Reports</i>. 2022;23(7). doi:<a href="https://doi.org/10.15252/embr.202154163">10.15252/embr.202154163</a> eng info:eu-repo/semantics/altIdentifier/doi/10.15252/embr.202154163 info:eu-repo/semantics/altIdentifier/issn/1469-221X info:eu-repo/semantics/altIdentifier/e-issn/1469-3178 info:eu-repo/semantics/altIdentifier/wos/000797302700001 info:eu-repo/semantics/altIdentifier/pmid/35586945 info:eu-repo/semantics/openAccess