RRC ID 76274
Author Rahman M, Ramirez-Suarez NJ, Diaz-Balzac CA, Bülow HE.
Title Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning.
Journal EMBO Rep
Abstract 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.
Volume 23(7)
Pages e54163
Published 2022-7-5
DOI 10.15252/embr.202154163
PMID 35586945
PMC PMC9253746
MeSH Amantadine / metabolism Animals Caenorhabditis elegans* / metabolism Caenorhabditis elegans Proteins* / metabolism Dendrites / metabolism Membrane Proteins / genetics Membrane Proteins / metabolism Polysaccharides / chemistry Polysaccharides / metabolism
Resource
C.elegans tm1078 tm5159