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Protein phase separation hotspots at the presynapse

Fundamental discoveries have shaped our molecular understanding of presynaptic processes, such as neurotransmitter release, active zone organization and mechanisms of synaptic vesicle (SV) recycling. However, certain regulatory steps still remain incompletely understood. Protein liquid–liquid phase...

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Detalles Bibliográficos
Autor principal: Lautenschläger, Janin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8826138/
https://www.ncbi.nlm.nih.gov/pubmed/35135293
http://dx.doi.org/10.1098/rsob.210334
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author Lautenschläger, Janin
author_facet Lautenschläger, Janin
author_sort Lautenschläger, Janin
collection PubMed
description Fundamental discoveries have shaped our molecular understanding of presynaptic processes, such as neurotransmitter release, active zone organization and mechanisms of synaptic vesicle (SV) recycling. However, certain regulatory steps still remain incompletely understood. Protein liquid–liquid phase separation (LLPS) and its role in SV clustering and active zone regulation now introduce a new perception of how the presynapse and its different compartments are organized. This article highlights the newly emerging concept of LLPS at the synapse, providing a systematic overview on LLPS tendencies of over 500 presynaptic proteins, spotlighting individual proteins and discussing recent progress in the field. Newly discovered LLPS systems like ELKS/liprin-alpha and Eps15/FCho are put into context, and further LLPS candidate proteins, including epsin1, dynamin, synaptojanin, complexin and rabphilin-3A, are highlighted.
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spelling pubmed-88261382022-02-10 Protein phase separation hotspots at the presynapse Lautenschläger, Janin Open Biol Review Fundamental discoveries have shaped our molecular understanding of presynaptic processes, such as neurotransmitter release, active zone organization and mechanisms of synaptic vesicle (SV) recycling. However, certain regulatory steps still remain incompletely understood. Protein liquid–liquid phase separation (LLPS) and its role in SV clustering and active zone regulation now introduce a new perception of how the presynapse and its different compartments are organized. This article highlights the newly emerging concept of LLPS at the synapse, providing a systematic overview on LLPS tendencies of over 500 presynaptic proteins, spotlighting individual proteins and discussing recent progress in the field. Newly discovered LLPS systems like ELKS/liprin-alpha and Eps15/FCho are put into context, and further LLPS candidate proteins, including epsin1, dynamin, synaptojanin, complexin and rabphilin-3A, are highlighted. The Royal Society 2022-02-09 /pmc/articles/PMC8826138/ /pubmed/35135293 http://dx.doi.org/10.1098/rsob.210334 Text en © 2022 The Authors. https://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, provided the original author and source are credited.
spellingShingle Review
Lautenschläger, Janin
Protein phase separation hotspots at the presynapse
title Protein phase separation hotspots at the presynapse
title_full Protein phase separation hotspots at the presynapse
title_fullStr Protein phase separation hotspots at the presynapse
title_full_unstemmed Protein phase separation hotspots at the presynapse
title_short Protein phase separation hotspots at the presynapse
title_sort protein phase separation hotspots at the presynapse
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8826138/
https://www.ncbi.nlm.nih.gov/pubmed/35135293
http://dx.doi.org/10.1098/rsob.210334
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