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The golgin family exhibits a propensity to form condensates in living cells

The Golgi is surrounded by a ribosome‐excluding matrix. Recently, we reported that the cis‐Golgi‐localized golgin GM130 can phase‐separate to form dynamic, liquid‐like condensates in vitro and in vivo. Here, we show that the overexpression of each of the remaining cis (golgin160, GMAP210)‐ and trans...

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Autores principales: Ziltener, Pascal, Rebane, Aleksander A., Graham, Morven, Ernst, Andreas M., Rothman, James E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7589415/
https://www.ncbi.nlm.nih.gov/pubmed/32668013
http://dx.doi.org/10.1002/1873-3468.13884
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author Ziltener, Pascal
Rebane, Aleksander A.
Graham, Morven
Ernst, Andreas M.
Rothman, James E.
author_facet Ziltener, Pascal
Rebane, Aleksander A.
Graham, Morven
Ernst, Andreas M.
Rothman, James E.
author_sort Ziltener, Pascal
collection PubMed
description The Golgi is surrounded by a ribosome‐excluding matrix. Recently, we reported that the cis‐Golgi‐localized golgin GM130 can phase‐separate to form dynamic, liquid‐like condensates in vitro and in vivo. Here, we show that the overexpression of each of the remaining cis (golgin160, GMAP210)‐ and trans (golgin97, golgin245, GCC88, GCC185)‐golgins results in novel protein condensates. Focused ion beam scanning electron microscopy (FIB‐SEM) images of GM130 condensates reveal a complex internal organization with branching aqueous channels. Pairs of golgins overexpressed in the same cell form distinct juxtaposed condensates. These findings support the hypothesis that, in addition to their established roles as vesicle tethers, phase separation may be a common feature of the golgin family that contributes to Golgi organization.
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spelling pubmed-75894152020-10-30 The golgin family exhibits a propensity to form condensates in living cells Ziltener, Pascal Rebane, Aleksander A. Graham, Morven Ernst, Andreas M. Rothman, James E. FEBS Lett Editor's Choice The Golgi is surrounded by a ribosome‐excluding matrix. Recently, we reported that the cis‐Golgi‐localized golgin GM130 can phase‐separate to form dynamic, liquid‐like condensates in vitro and in vivo. Here, we show that the overexpression of each of the remaining cis (golgin160, GMAP210)‐ and trans (golgin97, golgin245, GCC88, GCC185)‐golgins results in novel protein condensates. Focused ion beam scanning electron microscopy (FIB‐SEM) images of GM130 condensates reveal a complex internal organization with branching aqueous channels. Pairs of golgins overexpressed in the same cell form distinct juxtaposed condensates. These findings support the hypothesis that, in addition to their established roles as vesicle tethers, phase separation may be a common feature of the golgin family that contributes to Golgi organization. John Wiley and Sons Inc. 2020-08-02 2020-10 /pmc/articles/PMC7589415/ /pubmed/32668013 http://dx.doi.org/10.1002/1873-3468.13884 Text en © 2020 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Editor's Choice
Ziltener, Pascal
Rebane, Aleksander A.
Graham, Morven
Ernst, Andreas M.
Rothman, James E.
The golgin family exhibits a propensity to form condensates in living cells
title The golgin family exhibits a propensity to form condensates in living cells
title_full The golgin family exhibits a propensity to form condensates in living cells
title_fullStr The golgin family exhibits a propensity to form condensates in living cells
title_full_unstemmed The golgin family exhibits a propensity to form condensates in living cells
title_short The golgin family exhibits a propensity to form condensates in living cells
title_sort golgin family exhibits a propensity to form condensates in living cells
topic Editor's Choice
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7589415/
https://www.ncbi.nlm.nih.gov/pubmed/32668013
http://dx.doi.org/10.1002/1873-3468.13884
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