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Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection

SidE family of Legionella effectors catalyze non-canonical phosphoribosyl-linked ubiquitination (PR-ubiquitination) of host proteins during bacterial infection. SdeA localizes predominantly to ER and partially to the Golgi apparatus, and mediates serine ubiquitination of multiple ER and Golgi protei...

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Autores principales: Liu, Yaobin, Mukherjee, Rukmini, Bonn, Florian, Colby, Thomas, Matic, Ivan, Glogger, Marius, Heilemann, Mike, Dikic, Ivan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8481228/
https://www.ncbi.nlm.nih.gov/pubmed/34285384
http://dx.doi.org/10.1038/s41418-021-00830-y
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author Liu, Yaobin
Mukherjee, Rukmini
Bonn, Florian
Colby, Thomas
Matic, Ivan
Glogger, Marius
Heilemann, Mike
Dikic, Ivan
author_facet Liu, Yaobin
Mukherjee, Rukmini
Bonn, Florian
Colby, Thomas
Matic, Ivan
Glogger, Marius
Heilemann, Mike
Dikic, Ivan
author_sort Liu, Yaobin
collection PubMed
description SidE family of Legionella effectors catalyze non-canonical phosphoribosyl-linked ubiquitination (PR-ubiquitination) of host proteins during bacterial infection. SdeA localizes predominantly to ER and partially to the Golgi apparatus, and mediates serine ubiquitination of multiple ER and Golgi proteins. Here we show that SdeA causes disruption of Golgi integrity due to its ubiquitin ligase activity. The Golgi linking proteins GRASP55 and GRASP65 are PR-ubiquitinated on multiple serine residues, thus preventing their ability to cluster and form oligomeric structures. In addition, we found that the functional consequence of Golgi disruption is not linked to the recruitment of Golgi membranes to the growing Legionella-containing vacuoles. Instead, it affects the host secretory pathway. Taken together, our study sheds light on the Golgi manipulation strategy by which Legionella hijacks the secretory pathway and promotes bacterial infection.
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spelling pubmed-84812282021-10-08 Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection Liu, Yaobin Mukherjee, Rukmini Bonn, Florian Colby, Thomas Matic, Ivan Glogger, Marius Heilemann, Mike Dikic, Ivan Cell Death Differ Article SidE family of Legionella effectors catalyze non-canonical phosphoribosyl-linked ubiquitination (PR-ubiquitination) of host proteins during bacterial infection. SdeA localizes predominantly to ER and partially to the Golgi apparatus, and mediates serine ubiquitination of multiple ER and Golgi proteins. Here we show that SdeA causes disruption of Golgi integrity due to its ubiquitin ligase activity. The Golgi linking proteins GRASP55 and GRASP65 are PR-ubiquitinated on multiple serine residues, thus preventing their ability to cluster and form oligomeric structures. In addition, we found that the functional consequence of Golgi disruption is not linked to the recruitment of Golgi membranes to the growing Legionella-containing vacuoles. Instead, it affects the host secretory pathway. Taken together, our study sheds light on the Golgi manipulation strategy by which Legionella hijacks the secretory pathway and promotes bacterial infection. Nature Publishing Group UK 2021-07-20 2021-10 /pmc/articles/PMC8481228/ /pubmed/34285384 http://dx.doi.org/10.1038/s41418-021-00830-y Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Liu, Yaobin
Mukherjee, Rukmini
Bonn, Florian
Colby, Thomas
Matic, Ivan
Glogger, Marius
Heilemann, Mike
Dikic, Ivan
Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
title Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
title_full Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
title_fullStr Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
title_full_unstemmed Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
title_short Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
title_sort serine-ubiquitination regulates golgi morphology and the secretory pathway upon legionella infection
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8481228/
https://www.ncbi.nlm.nih.gov/pubmed/34285384
http://dx.doi.org/10.1038/s41418-021-00830-y
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