Academic Journal

Molecular Organization and Regulation of the Mammalian Synapse by the Post-Translational Modification SUMOylation

التفاصيل البيبلوغرافية
العنوان: Molecular Organization and Regulation of the Mammalian Synapse by the Post-Translational Modification SUMOylation
المؤلفون: Chato-Astrain, Isabel, Pronot, Marie, Coppola, Thierry, Martin, Stéphane
المساهمون: Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (1965 - 2019) (UNS)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UniCA), University of Edinburgh (Edin.), Université Côte d'Azur (UniCA), ANR-20-CE16-0006,InnoVinFXS,Explorer des stratégies innovantes pour restaurer la fonction synaptique et les comportements sociocognitifs dans un modèle murin exprimant une mutation récurrente du syndrome du X fragile chez l'humain(2020)
المصدر: ISSN: 2073-4409 ; Cells ; https://inserm.hal.science/inserm-04513386 ; Cells, 2024, 13 (5), pp.420. ⟨10.3390/cells13050420⟩.
بيانات النشر: HAL CCSD
MDPI
سنة النشر: 2024
المجموعة: HAL Université Côte d'Azur
مصطلحات موضوعية: LLPS, SUMO, SUMOylation, biomolecular condensate, post-translational modification, synapse, [SDV]Life Sciences [q-bio]
الوصف: International audience ; Neurotransmission occurs within highly specialized compartments forming the active synapse where the complex organization and dynamics of the interactions are tightly orchestrated both in time and space. Post-translational modifications (PTMs) are central to these spatiotemporal regulations to ensure an efficient synaptic transmission. SUMOylation is a dynamic PTM that modulates the interactions between proteins and consequently regulates the conformation, the distribution and the trafficking of the SUMO-target proteins. SUMOylation plays a crucial role in synapse formation and stabilization, as well as in the regulation of synaptic transmission and plasticity. In this review, we summarize the molecular consequences of this protein modification in the structural organization and function of the mammalian synapse. We also outline novel activity-dependent regulation and consequences of the SUMO process and explore how this protein modification can functionally participate in the compartmentalization of both pre- and post-synaptic sites.
نوع الوثيقة: article in journal/newspaper
اللغة: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/38474384; inserm-04513386; https://inserm.hal.science/inserm-04513386; PUBMED: 38474384; PUBMEDCENTRAL: PMC10930594
DOI: 10.3390/cells13050420
الاتاحة: https://inserm.hal.science/inserm-04513386
https://doi.org/10.3390/cells13050420
رقم الانضمام: edsbas.E32733C9
قاعدة البيانات: BASE