Abstract |
The intracellular bacterial pathogen Legionella pneumophila subverts host membrane transport pathways to promote fusion of vesicles exiting the endoplasmic reticulum (ER) with the pathogen-containing vacuole. During infection there is noncanonical pairing of the SNARE protein Sec22b on ER-derived vesicles with plasma membrane (PM)-localized syntaxin proteins on the vacuole. We show that the L. pneumophila Rab1-targeting effector DrrA is sufficient to stimulate this noncanonical SNARE association and promote membrane fusion. DrrA activation of the Rab1 GTPase on PM-derived organelles stimulated the tethering of ER-derived vesicles with the PM-derived organelle, resulting in vesicle fusion through the pairing of Sec22b with the PM syntaxin proteins. Thus, the effector protein DrrA stimulates a host membrane transport pathway that enables ER-derived vesicles to remodel a PM-derived organelle, suggesting that Rab1 activation at the PM is sufficient to promote the recruitment and fusion of ER-derived vesicles.
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Authors | Kohei Arasaki, Derek K Toomre, Craig R Roy |
Journal | Cell host & microbe
(Cell Host Microbe)
Vol. 11
Issue 1
Pg. 46-57
(Jan 19 2012)
ISSN: 1934-6069 [Electronic] United States |
PMID | 22264512
(Publication Type: Journal Article, Research Support, N.I.H., Extramural)
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Copyright | Copyright © 2012 Elsevier Inc. All rights reserved. |
Chemical References |
- Bacterial Proteins
- Guanine Nucleotide Exchange Factors
- Qa-SNARE Proteins
- R-SNARE Proteins
- Sec22B protein, human
- SidM protein, Legionella pneumophila
- rab1 GTP-Binding Proteins
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Topics |
- Bacterial Proteins
(metabolism)
- Cell Line
- Endoplasmic Reticulum
(metabolism)
- Guanine Nucleotide Exchange Factors
(metabolism)
- Humans
- Legionella pneumophila
(pathogenicity)
- Membrane Fusion
- Protein Binding
- Qa-SNARE Proteins
(metabolism)
- R-SNARE Proteins
(metabolism)
- Vacuoles
(metabolism, microbiology)
- rab1 GTP-Binding Proteins
(metabolism)
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