HOMEPRODUCTSCOMPANYCONTACTFAQResearchDictionaryPharmaSign Up FREE or Login

The Legionella pneumophila effector DrrA is sufficient to stimulate SNARE-dependent membrane fusion.

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.
AuthorsKohei Arasaki, Derek K Toomre, Craig R Roy
JournalCell host & microbe (Cell Host Microbe) Vol. 11 Issue 1 Pg. 46-57 (Jan 19 2012) ISSN: 1934-6069 [Electronic] United States
PMID22264512 (Publication Type: Journal Article, Research Support, N.I.H., Extramural)
CopyrightCopyright © 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
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)

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research graph!


Choose Username:
Email:
Password:
Verify Password:
Enter Code Shown: