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Synapsin E-domain is essential for α-synuclein function
The cytosolic proteins synucleins and synapsins are thought to play cooperative roles in regulating synaptic vesicle (SV) recycling, but mechanistic insight is lacking. Here we identify the synapsin E-domain as an essential functional binding-partner of α-synuclein (α-syn). Synapsin E-domain allows...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10327093/ https://www.ncbi.nlm.nih.gov/pubmed/37425805 http://dx.doi.org/10.1101/2023.06.24.546170 |
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author | Stavsky, Alexandra Parra-Rivas, Leonardo A. Tal, Shani Madhivanan, Kayalvizhi Roy, Subhojit Gitler, Daniel |
author_facet | Stavsky, Alexandra Parra-Rivas, Leonardo A. Tal, Shani Madhivanan, Kayalvizhi Roy, Subhojit Gitler, Daniel |
author_sort | Stavsky, Alexandra |
collection | PubMed |
description | The cytosolic proteins synucleins and synapsins are thought to play cooperative roles in regulating synaptic vesicle (SV) recycling, but mechanistic insight is lacking. Here we identify the synapsin E-domain as an essential functional binding-partner of α-synuclein (α-syn). Synapsin E-domain allows α-syn functionality, binds to α-syn, and is necessary and sufficient for enabling effects of α-syn at the synapse. Together with previous studies implicating the E-domain in clustering SVs, our experiments advocate a cooperative role for these two proteins in maintaining physiologic SV clusters. |
format | Online Article Text |
id | pubmed-10327093 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-103270932023-07-08 Synapsin E-domain is essential for α-synuclein function Stavsky, Alexandra Parra-Rivas, Leonardo A. Tal, Shani Madhivanan, Kayalvizhi Roy, Subhojit Gitler, Daniel bioRxiv Article The cytosolic proteins synucleins and synapsins are thought to play cooperative roles in regulating synaptic vesicle (SV) recycling, but mechanistic insight is lacking. Here we identify the synapsin E-domain as an essential functional binding-partner of α-synuclein (α-syn). Synapsin E-domain allows α-syn functionality, binds to α-syn, and is necessary and sufficient for enabling effects of α-syn at the synapse. Together with previous studies implicating the E-domain in clustering SVs, our experiments advocate a cooperative role for these two proteins in maintaining physiologic SV clusters. Cold Spring Harbor Laboratory 2023-06-26 /pmc/articles/PMC10327093/ /pubmed/37425805 http://dx.doi.org/10.1101/2023.06.24.546170 Text en https://creativecommons.org/licenses/by/4.0/This work is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. |
spellingShingle | Article Stavsky, Alexandra Parra-Rivas, Leonardo A. Tal, Shani Madhivanan, Kayalvizhi Roy, Subhojit Gitler, Daniel Synapsin E-domain is essential for α-synuclein function |
title | Synapsin E-domain is essential for α-synuclein function |
title_full | Synapsin E-domain is essential for α-synuclein function |
title_fullStr | Synapsin E-domain is essential for α-synuclein function |
title_full_unstemmed | Synapsin E-domain is essential for α-synuclein function |
title_short | Synapsin E-domain is essential for α-synuclein function |
title_sort | synapsin e-domain is essential for α-synuclein function |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10327093/ https://www.ncbi.nlm.nih.gov/pubmed/37425805 http://dx.doi.org/10.1101/2023.06.24.546170 |
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