Cargando…
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...
Autor principal: | |
---|---|
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 |
_version_ | 1784647369471557632 |
---|---|
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. |
format | Online Article Text |
id | pubmed-8826138 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT lautenschlagerjanin proteinphaseseparationhotspotsatthepresynapse |