高尔基体
长时程增强
细胞生物学
突触可塑性
神经细胞粘附分子
糖基化
突触
生物
神经科学
化学
细胞
生物化学
内质网
细胞粘附
受体
作者
Maria Andres‐Alonso,Maximilian Borgmeyer,Hadi Mirzapourdelavar,Jakob Lormann,Kim Klein,Michaela Schweizer,Sabine Hoffmeister‐Ullerich,Anja Maria Oelschlegel,Alexander E. Dityatev,Michael R. Kreutz
出处
期刊:Cell Reports
[Cell Press]
日期:2023-06-24
卷期号:42 (7): 112692-112692
被引量:17
标识
DOI:10.1016/j.celrep.2023.112692
摘要
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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