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, Vol. 42, No. 7, 112692, 25.07.2023.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Andres-Alonso, M, Borgmeyer, M, Mirzapourdelavar, H, Lormann, J, Klein, K, Schweizer, M, Hoffmeister-Ullerich, S, Oelschlegel, AM, Dityatev, A & Kreutz, MR 2023, 'Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses', CELL REP, vol. 42, no. 7, 112692. https://doi.org/10.1016/j.celrep.2023.112692

APA

Andres-Alonso, M., Borgmeyer, M., Mirzapourdelavar, H., Lormann, J., Klein, K., Schweizer, M., Hoffmeister-Ullerich, S., Oelschlegel, A. M., Dityatev, A., & Kreutz, M. R. (2023). Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses. CELL REP, 42(7), [112692]. https://doi.org/10.1016/j.celrep.2023.112692

Vancouver

Bibtex

@article{38f302b904bd4631aea17b27c93ce47f,
title = "Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses",
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.",
author = "Maria Andres-Alonso and Maximilian Borgmeyer and Hadi Mirzapourdelavar and Jakob Lormann and Kim Klein and Michaela Schweizer and Sabine Hoffmeister-Ullerich and Oelschlegel, {Anja M} and Alexander Dityatev and Kreutz, {Michael R}",
note = "Copyright {\textcopyright} 2023 The Author(s). Published by Elsevier Inc. All rights reserved.",
year = "2023",
month = jul,
day = "25",
doi = "10.1016/j.celrep.2023.112692",
language = "English",
volume = "42",
journal = "CELL REP",
issn = "2211-1247",
publisher = "Elsevier",
number = "7",

}

RIS

TY - JOUR

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 -