Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses
Summary: 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...
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Format: | Article |
Language: | English |
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Elsevier
2023-07-01
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Series: | Cell Reports |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124723007039 |
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author | Maria Andres-Alonso Maximilian Borgmeyer Hadi Mirzapourdelavar Jakob Lormann Kim Klein Michaela Schweizer Sabine Hoffmeister-Ullerich Anja M. Oelschlegel Alexander Dityatev Michael R. Kreutz |
author_facet | Maria Andres-Alonso Maximilian Borgmeyer Hadi Mirzapourdelavar Jakob Lormann Kim Klein Michaela Schweizer Sabine Hoffmeister-Ullerich Anja M. Oelschlegel Alexander Dityatev Michael R. Kreutz |
author_sort | Maria Andres-Alonso |
collection | DOAJ |
description | Summary: 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. |
first_indexed | 2024-03-13T03:28:45Z |
format | Article |
id | doaj.art-cc25592f2ad74310b045450eed535d52 |
institution | Directory Open Access Journal |
issn | 2211-1247 |
language | English |
last_indexed | 2024-03-13T03:28:45Z |
publishDate | 2023-07-01 |
publisher | Elsevier |
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series | Cell Reports |
spelling | doaj.art-cc25592f2ad74310b045450eed535d522023-06-25T04:42:53ZengElsevierCell Reports2211-12472023-07-01427112692Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapsesMaria Andres-Alonso0Maximilian Borgmeyer1Hadi Mirzapourdelavar2Jakob Lormann3Kim Klein4Michaela Schweizer5Sabine Hoffmeister-Ullerich6Anja M. Oelschlegel7Alexander Dityatev8Michael R. Kreutz9Leibniz Group “Dendritic Organelles and Synaptic Function,” Center for Molecular Neurobiology (ZMNH), University Medical Center Hamburg-Eppendorf, 20251 Hamburg, Germany; RG Neuroplasticity, Leibniz Institute for Neurobiology, 39118 Magdeburg, Germany; Corresponding authorLeibniz Group “Dendritic Organelles and Synaptic Function,” Center for Molecular Neurobiology (ZMNH), University Medical Center Hamburg-Eppendorf, 20251 Hamburg, Germany; RG Neuroplasticity, Leibniz Institute for Neurobiology, 39118 Magdeburg, GermanyGerman Center for Neurodegenerative Diseases (DZNE), 39120 Magdeburg, GermanyLeibniz Group “Dendritic Organelles and Synaptic Function,” Center for Molecular Neurobiology (ZMNH), University Medical Center Hamburg-Eppendorf, 20251 Hamburg, Germany; RG Neuroplasticity, Leibniz Institute for Neurobiology, 39118 Magdeburg, GermanyLeibniz Group “Dendritic Organelles and Synaptic Function,” Center for Molecular Neurobiology (ZMNH), University Medical Center Hamburg-Eppendorf, 20251 Hamburg, GermanyCore Facility Morphology und Electron Microscopy, Center for Molecular Neurobiology (ZMNH), University Medical Center Hamburg-Eppendorf, 20251 Hamburg, GermanyCore Facility Bioanalytik, Center for Molecular Neurobiology (ZMNH), University Medical Center Hamburg-Eppendorf, 20251 Hamburg, GermanyRG Neuroplasticity, Leibniz Institute for Neurobiology, 39118 Magdeburg, GermanyGerman Center for Neurodegenerative Diseases (DZNE), 39120 Magdeburg, Germany; Center for Behavioral Brain Sciences, Otto von Guericke University, 39120 Magdeburg, Germany; Medical Faculty, Otto von Guericke University, 39120 Magdeburg, GermanyLeibniz Group “Dendritic Organelles and Synaptic Function,” Center for Molecular Neurobiology (ZMNH), University Medical Center Hamburg-Eppendorf, 20251 Hamburg, Germany; RG Neuroplasticity, Leibniz Institute for Neurobiology, 39118 Magdeburg, Germany; German Center for Neurodegenerative Diseases (DZNE), 39120 Magdeburg, Germany; Center for Behavioral Brain Sciences, Otto von Guericke University, 39120 Magdeburg, Germany; Corresponding authorSummary: 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.http://www.sciencedirect.com/science/article/pii/S2211124723007039CP: Cell biologyCP: Neuroscience |
spellingShingle | Maria Andres-Alonso Maximilian Borgmeyer Hadi Mirzapourdelavar Jakob Lormann Kim Klein Michaela Schweizer Sabine Hoffmeister-Ullerich Anja M. Oelschlegel Alexander Dityatev Michael R. Kreutz Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses Cell Reports CP: Cell biology CP: Neuroscience |
title | Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses |
title_full | Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses |
title_fullStr | Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses |
title_full_unstemmed | Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses |
title_short | Golgi satellites are essential for polysialylation of NCAM and expression of LTP at distal synapses |
title_sort | golgi satellites are essential for polysialylation of ncam and expression of ltp at distal synapses |
topic | CP: Cell biology CP: Neuroscience |
url | http://www.sciencedirect.com/science/article/pii/S2211124723007039 |
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