Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses
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Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses. / Andres-Alonso, Maria; Borgmeyer, Maximilian; Mirzapourdelavar, Hadi; Lormann, Jakob; Klein, Kim; Schweizer, Michaela; Hoffmeister-Ullerich, Sabine; Oelschlegel, Anja M; Dityatev, Alexander; Kreutz, Michael R.
in: CELL REP, Jahrgang 42, Nr. 7, 112692, 25.07.2023.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses
AU - Andres-Alonso, Maria
AU - Borgmeyer, Maximilian
AU - Mirzapourdelavar, Hadi
AU - Lormann, Jakob
AU - Klein, Kim
AU - Schweizer, Michaela
AU - Hoffmeister-Ullerich, Sabine
AU - Oelschlegel, Anja M
AU - Dityatev, Alexander
AU - Kreutz, Michael R
N1 - Copyright © 2023 The Author(s). Published by Elsevier Inc. All rights reserved.
PY - 2023/7/25
Y1 - 2023/7/25
N2 - 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.
AB - 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.
U2 - 10.1016/j.celrep.2023.112692
DO - 10.1016/j.celrep.2023.112692
M3 - SCORING: Journal article
C2 - 37355986
VL - 42
JO - CELL REP
JF - CELL REP
SN - 2211-1247
IS - 7
M1 - 112692
ER -