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The sorting of cargo proteins in the plant trans-Golgi network

Membrane trafficking contributes to distinct protein compositions of organelles and is essential for proper organellar maintenance and functions. The trans-Golgi network (TGN) acts as a sorting station where various cargo proteins are sorted and directed to post-Golgi compartments, such as the multi...

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Detalles Bibliográficos
Autores principales: Shimizu, Yutaro, Uemura, Tomohiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9402974/
https://www.ncbi.nlm.nih.gov/pubmed/36035717
http://dx.doi.org/10.3389/fpls.2022.957995
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author Shimizu, Yutaro
Uemura, Tomohiro
author_facet Shimizu, Yutaro
Uemura, Tomohiro
author_sort Shimizu, Yutaro
collection PubMed
description Membrane trafficking contributes to distinct protein compositions of organelles and is essential for proper organellar maintenance and functions. The trans-Golgi network (TGN) acts as a sorting station where various cargo proteins are sorted and directed to post-Golgi compartments, such as the multivesicular body or pre-vacuolar compartment, vacuoles, and plasma membrane. The spatial and temporal segregation of cargo proteins within the TGN, which is mediated with different sets of regulators including small GTPases and cargo adaptors, is a fundamental process in the sorting machinery. Recent studies with powerful imaging technologies have suggested that the TGN possesses spatially distinct subdomains or zones for different trafficking pathways. In this review, we will summarize the spatially and dynamically characteristic features of the plant TGN and their relation to cargo protein trafficking.
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spelling pubmed-94029742022-08-26 The sorting of cargo proteins in the plant trans-Golgi network Shimizu, Yutaro Uemura, Tomohiro Front Plant Sci Plant Science Membrane trafficking contributes to distinct protein compositions of organelles and is essential for proper organellar maintenance and functions. The trans-Golgi network (TGN) acts as a sorting station where various cargo proteins are sorted and directed to post-Golgi compartments, such as the multivesicular body or pre-vacuolar compartment, vacuoles, and plasma membrane. The spatial and temporal segregation of cargo proteins within the TGN, which is mediated with different sets of regulators including small GTPases and cargo adaptors, is a fundamental process in the sorting machinery. Recent studies with powerful imaging technologies have suggested that the TGN possesses spatially distinct subdomains or zones for different trafficking pathways. In this review, we will summarize the spatially and dynamically characteristic features of the plant TGN and their relation to cargo protein trafficking. Frontiers Media S.A. 2022-08-11 /pmc/articles/PMC9402974/ /pubmed/36035717 http://dx.doi.org/10.3389/fpls.2022.957995 Text en Copyright © 2022 Shimizu and Uemura. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Shimizu, Yutaro
Uemura, Tomohiro
The sorting of cargo proteins in the plant trans-Golgi network
title The sorting of cargo proteins in the plant trans-Golgi network
title_full The sorting of cargo proteins in the plant trans-Golgi network
title_fullStr The sorting of cargo proteins in the plant trans-Golgi network
title_full_unstemmed The sorting of cargo proteins in the plant trans-Golgi network
title_short The sorting of cargo proteins in the plant trans-Golgi network
title_sort sorting of cargo proteins in the plant trans-golgi network
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9402974/
https://www.ncbi.nlm.nih.gov/pubmed/36035717
http://dx.doi.org/10.3389/fpls.2022.957995
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