TY - JOUR
T1 - Specific N-glycans regulate an extracellular adhesion complex during somatosensory dendrite patterning
AU - Rahman, Maisha
AU - Ramirez-Suarez, Nelson J.
AU - Diaz-Balzac, Carlos A.
AU - Bülow, Hannes E.
N1 - Publisher Copyright:
© 2022 The Authors.
PY - 2022/7/5
Y1 - 2022/7/5
N2 - 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.
AB - 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.
KW - N-glycans
KW - adhesion
KW - alpha mannosidase II
KW - dendrite
KW - glycosylations
UR - http://www.scopus.com/inward/record.url?scp=85130277315&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85130277315&partnerID=8YFLogxK
U2 - 10.15252/embr.202154163
DO - 10.15252/embr.202154163
M3 - Article
C2 - 35586945
AN - SCOPUS:85130277315
SN - 1469-221X
VL - 23
JO - EMBO Reports
JF - EMBO Reports
IS - 7
M1 - e54163
ER -