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Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins

More than 2 decades of work have yet to conclusively determine the physiological role of the synuclein proteins, even though these abundant brain constituents are participants in a broad array of cellular processes. Among proposed physiological roles is a functional interaction between the synuclein...

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Detalles Bibliográficos
Autores principales: Oaks, Adam W, Sidhu, Anita
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3917945/
https://www.ncbi.nlm.nih.gov/pubmed/24563712
http://dx.doi.org/10.4161/cib.26794
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author Oaks, Adam W
Sidhu, Anita
author_facet Oaks, Adam W
Sidhu, Anita
author_sort Oaks, Adam W
collection PubMed
description More than 2 decades of work have yet to conclusively determine the physiological role of the synuclein proteins, even though these abundant brain constituents are participants in a broad array of cellular processes. Among proposed physiological roles is a functional interaction between the synuclein proteins and monoamine transporters contributing to transporter trafficking through direct protein–protein interactions. Recent work shows that an antagonistic effect of the synuclein proteins on the secretory functions of the endoplasmic reticulum and the Golgi apparatus appears to simultaneously influence trafficking of the dopamine transporter and other membrane proteins. Here, we highlight these new findings in view of the broader literature identifying the role of synucleins in protein trafficking and suggest emerging themes for ongoing and future work in the field of synuclein biology.
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spelling pubmed-39179452014-02-21 Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins Oaks, Adam W Sidhu, Anita Commun Integr Biol Mini Review More than 2 decades of work have yet to conclusively determine the physiological role of the synuclein proteins, even though these abundant brain constituents are participants in a broad array of cellular processes. Among proposed physiological roles is a functional interaction between the synuclein proteins and monoamine transporters contributing to transporter trafficking through direct protein–protein interactions. Recent work shows that an antagonistic effect of the synuclein proteins on the secretory functions of the endoplasmic reticulum and the Golgi apparatus appears to simultaneously influence trafficking of the dopamine transporter and other membrane proteins. Here, we highlight these new findings in view of the broader literature identifying the role of synucleins in protein trafficking and suggest emerging themes for ongoing and future work in the field of synuclein biology. Landes Bioscience 2013-11-01 2013-11-13 /pmc/articles/PMC3917945/ /pubmed/24563712 http://dx.doi.org/10.4161/cib.26794 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Mini Review
Oaks, Adam W
Sidhu, Anita
Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins
title Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins
title_full Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins
title_fullStr Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins
title_full_unstemmed Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins
title_short Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins
title_sort parallel mechanisms for direct and indirect membrane protein trafficking by synucleins
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3917945/
https://www.ncbi.nlm.nih.gov/pubmed/24563712
http://dx.doi.org/10.4161/cib.26794
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