Organization of Presynaptic Autophagy-Related Processes.

Bassoon active zone (AZ) amphisome autophagy endocytic zone endolysosomal system presynaptic proteostasis synaptic vesicle (SV)

Journal

Frontiers in synaptic neuroscience
ISSN: 1663-3563
Titre abrégé: Front Synaptic Neurosci
Pays: Switzerland
ID NLM: 101548972

Informations de publication

Date de publication:
2022
Historique:
received: 05 12 2021
accepted: 04 01 2022
entrez: 4 4 2022
pubmed: 5 4 2022
medline: 5 4 2022
Statut: epublish

Résumé

Brain synapses pose special challenges on the quality control of their protein machineries as they are far away from the neuronal soma, display a high potential for plastic adaptation and have a high energy demand to fulfill their physiological tasks. This applies in particular to the presynaptic part where neurotransmitter is released from synaptic vesicles, which in turn have to be recycled and refilled in a complex membrane trafficking cycle. Pathways to remove outdated and damaged proteins include the ubiquitin-proteasome system acting in the cytoplasm as well as membrane-associated endolysosomal and the autophagy systems. Here we focus on the latter systems and review what is known about the spatial organization of autophagy and endolysomal processes within the presynapse. We provide an inventory of which components of these degradative systems were found to be present in presynaptic boutons and where they might be anchored to the presynaptic apparatus. We identify three presynaptic structures reported to interact with known constituents of membrane-based protein-degradation pathways and therefore may serve as docking stations. These are (i) scaffolding proteins of the cytomatrix at the active zone, such as Bassoon or Clarinet, (ii) the endocytic machinery localized mainly at the peri-active zone, and (iii) synaptic vesicles. Finally, we sketch scenarios, how presynaptic autophagic cargos are tagged and recruited and which cellular mechanisms may govern membrane-associated protein turnover in the presynapse.

Identifiants

pubmed: 35368245
doi: 10.3389/fnsyn.2022.829354
pmc: PMC8968026
doi:

Types de publication

Journal Article Review

Langues

eng

Pagination

829354

Informations de copyright

Copyright © 2022 Gundelfinger, Karpova, Pielot, Garner and Kreutz.

Déclaration de conflit d'intérêts

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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Auteurs

Eckart D Gundelfinger (ED)

Research Group Neuroplasticity, Leibniz Institute for Neurobiology, Magdeburg, Germany.
Institute of Pharmacology and Toxicology, Medical Faculty, Otto von Guericke University, Magdeburg, Germany.
Center for Behavioral Brain Sciences (CBBS), Magdeburg, Germany.

Anna Karpova (A)

Research Group Neuroplasticity, Leibniz Institute for Neurobiology, Magdeburg, Germany.
Center for Behavioral Brain Sciences (CBBS), Magdeburg, Germany.

Rainer Pielot (R)

Institute of Pharmacology and Toxicology, Medical Faculty, Otto von Guericke University, Magdeburg, Germany.
Center for Behavioral Brain Sciences (CBBS), Magdeburg, Germany.

Craig C Garner (CC)

German Center for Neurodegenerative Diseases (DZNE), Berlin, Germany.
Charité - Universitätsmedizin Berlin, Berlin, Germany.

Michael R Kreutz (MR)

Research Group Neuroplasticity, Leibniz Institute for Neurobiology, Magdeburg, Germany.
Center for Behavioral Brain Sciences (CBBS), Magdeburg, Germany.
Center for Molecular Neurobiology (ZMNH), University Hospital Hamburg-Eppendorf, Hamburg, Germany.
German Center for Neurodegenerative Diseases (DZNE), Magdeburg, Germany.

Classifications MeSH