Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
© 2021. The Author(s)..
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:28 |
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| Enthalten in: |
Cell death and differentiation - 28(2021), 10 vom: 20. Okt., Seite 2957-2969 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Liu, Yaobin [VerfasserIn] |
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| Links: |
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| Themen: |
452VLY9402 |
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| Anmerkungen: |
Date Completed 25.03.2022 Date Revised 21.07.2022 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1038/s41418-021-00830-y |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM328304980 |
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| 520 | |a © 2021. The Author(s). | ||
| 520 | |a 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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| 700 | 1 | |a Matic, Ivan |e verfasserin |4 aut | |
| 700 | 1 | |a Glogger, Marius |e verfasserin |4 aut | |
| 700 | 1 | |a Heilemann, Mike |e verfasserin |4 aut | |
| 700 | 1 | |a Dikic, Ivan |e verfasserin |4 aut | |
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