Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection.
Journal
Cell death and differentiation
ISSN: 1476-5403
Titre abrégé: Cell Death Differ
Pays: England
ID NLM: 9437445
Informations de publication
Date de publication:
10 2021
10 2021
Historique:
received:
03
03
2021
accepted:
05
07
2021
revised:
02
07
2021
pubmed:
22
7
2021
medline:
26
3
2022
entrez:
21
7
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 34285384
doi: 10.1038/s41418-021-00830-y
pii: 10.1038/s41418-021-00830-y
pmc: PMC8481228
doi:
Substances chimiques
Serine
452VLY9402
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2957-2969Subventions
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : EXC 2030-390661388
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 253130777
Organisme : EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council)
ID : 742720
Informations de copyright
© 2021. The Author(s).
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