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Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
- Source :
- Cell Death & Differntiation, Cell Death Differ, Cell Death and Differentiation
- Publication Year :
- 2021
-
Abstract
- 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 secretory pathway, including cytokine release in cells. Taken together, our study sheds light on the Golgi manipulation strategy by which Legionella hijacks the secretory pathway and promotes bacterial infection.
- Subjects :
- Legionella
medicine.medical_treatment
Golgi Apparatus
Vacuole
Biochemistry
Article
Serine
03 medical and health sciences
symbols.namesake
0302 clinical medicine
Ubiquitin
ddc:570
medicine
Humans
ddc:610
Fragmentation (cell biology)
Molecular Biology
Secretory pathway
Host protein
030304 developmental biology
0303 health sciences
biology
Effector
Chemistry
Ubiquitination
Cell Biology
Golgi apparatus
biology.organism_classification
Cell biology
Cytokine
symbols
biology.protein
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 13509047
- Database :
- OpenAIRE
- Journal :
- Cell Death & Differntiation
- Accession number :
- edsair.doi.dedup.....1314e556357c606cf8a03d693481faa4
- Full Text :
- https://doi.org/10.1038/s41418-021-00830-y