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Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport

Secretory cargo is recognized, concentrated and trafficked from endoplasmic reticulum (ER) exit sites (ERES) to the Golgi. Cargo export from the ER begins when a series of highly conserved COPII coat proteins accumulate at the ER and regulate the formation of cargo-loaded COPII vesicles. In animal c...

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Autores principales: Westrate, Laura M., Hoyer, Melissa J., Nash, Michael J., Voeltz, Gia K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7390636/
https://www.ncbi.nlm.nih.gov/pubmed/32616562
http://dx.doi.org/10.1242/jcs.239814
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author Westrate, Laura M.
Hoyer, Melissa J.
Nash, Michael J.
Voeltz, Gia K.
author_facet Westrate, Laura M.
Hoyer, Melissa J.
Nash, Michael J.
Voeltz, Gia K.
author_sort Westrate, Laura M.
collection PubMed
description Secretory cargo is recognized, concentrated and trafficked from endoplasmic reticulum (ER) exit sites (ERES) to the Golgi. Cargo export from the ER begins when a series of highly conserved COPII coat proteins accumulate at the ER and regulate the formation of cargo-loaded COPII vesicles. In animal cells, capturing live de novo cargo trafficking past this point is challenging; it has been difficult to discriminate whether cargo is trafficked to the Golgi in a COPII-coated vesicle. Here, we describe a recently developed live-cell cargo export system that can be synchronously released from ERES to illustrate de novo trafficking in animal cells. We found that components of the COPII coat remain associated with the ERES while cargo is extruded into COPII-uncoated, non-ER associated, Rab1 (herein referring to Rab1a or Rab1b)-dependent carriers. Our data suggest that, in animal cells, COPII coat components remain stably associated with the ER at exit sites to generate a specialized compartment, but once cargo is sorted and organized, Rab1 labels these export carriers and facilitates efficient forward trafficking. This article has an associated First Person interview with the first author of the paper.
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spelling pubmed-73906362020-08-05 Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport Westrate, Laura M. Hoyer, Melissa J. Nash, Michael J. Voeltz, Gia K. J Cell Sci Research Article Secretory cargo is recognized, concentrated and trafficked from endoplasmic reticulum (ER) exit sites (ERES) to the Golgi. Cargo export from the ER begins when a series of highly conserved COPII coat proteins accumulate at the ER and regulate the formation of cargo-loaded COPII vesicles. In animal cells, capturing live de novo cargo trafficking past this point is challenging; it has been difficult to discriminate whether cargo is trafficked to the Golgi in a COPII-coated vesicle. Here, we describe a recently developed live-cell cargo export system that can be synchronously released from ERES to illustrate de novo trafficking in animal cells. We found that components of the COPII coat remain associated with the ERES while cargo is extruded into COPII-uncoated, non-ER associated, Rab1 (herein referring to Rab1a or Rab1b)-dependent carriers. Our data suggest that, in animal cells, COPII coat components remain stably associated with the ER at exit sites to generate a specialized compartment, but once cargo is sorted and organized, Rab1 labels these export carriers and facilitates efficient forward trafficking. This article has an associated First Person interview with the first author of the paper. The Company of Biologists Ltd 2020-07-24 /pmc/articles/PMC7390636/ /pubmed/32616562 http://dx.doi.org/10.1242/jcs.239814 Text en © 2020. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/4.0This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
spellingShingle Research Article
Westrate, Laura M.
Hoyer, Melissa J.
Nash, Michael J.
Voeltz, Gia K.
Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport
title Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport
title_full Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport
title_fullStr Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport
title_full_unstemmed Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport
title_short Vesicular and uncoated Rab1-dependent cargo carriers facilitate ER to Golgi transport
title_sort vesicular and uncoated rab1-dependent cargo carriers facilitate er to golgi transport
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7390636/
https://www.ncbi.nlm.nih.gov/pubmed/32616562
http://dx.doi.org/10.1242/jcs.239814
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