Journal
CELL REPORTS
Volume 42, Issue 7, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2023.112692
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The complex structure of neurons presents challenges for the maturation of synaptic membrane proteins. Golgi-satellites (GSs) are distributed along dendrites and can perform mature glycosylation, particularly sialylation. GSs polysialylate locally secreted NCAM, and their reduction leads to decreased levels of PSA-NCAM in distal dendrites and impaired long-term potentiation.
The complex cytoarchitecture of neurons poses significant challenges for the maturation of synaptic membrane proteins. It is currently unclear whether locally secreted synaptic proteins bypass the Golgi or whether they traffic through Golgi satellites (GSs). Here, we create a transgenic GS reporter mouse line and show that GSs are widely distributed along dendrites and are capable of mature glycosylation, in particular sialylation. We find that polysialylation of locally secreted NCAM takes place at GSs. Accordingly, in mice lacking a component of trans-Golgi network-to-plasma membrane trafficking, we find fewer GSs and significantly reduced PSA-NCAM levels in distal dendrites of CA1 neurons that receive input from the temporoammonic pathway. Induction of long-term potentiation at those, but not more proximal, synapses is severely impaired. We conclude that GSs serve the need for local mature glycosylation of synaptic membrane proteins in distal dendrites and thereby contribute to rapid changes in synaptic strength.
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