Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses

Cell Rep. 2023 Jul 25;42(7):112692. doi: 10.1016/j.celrep.2023.112692. Epub 2023 Jun 24.

Abstract

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.

Keywords: CP: Cell biology; CP: Neuroscience; Golgi satellites; NCAM; polysialylation; secretory trafficking; synaptic plasticity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Dendrites / metabolism
  • Long-Term Potentiation* / physiology
  • Mice
  • Neural Cell Adhesion Molecules / metabolism
  • Neurons / metabolism
  • Synapses* / metabolism

Substances

  • Neural Cell Adhesion Molecules