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- Title
The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor.
- Authors
Murata, Takahiro; Delprato, Anna; Ingmundson, Alyssa; Toomre, Derek K.; Lambright, David G.; Roy, Craig R.
- Abstract
The intracellular pathogen Legionella pneumophila avoids fusion with lysosomes and subverts membrane transport from the endoplasmic reticulum to create an organelle that supports bacterial replication. Transport of endoplasmic reticulum-derived vesicles to the Legionella-containing vacuole (LCV) requires bacterial proteins that are translocated into host cells by a type IV secretion apparatus called Dot/Icm. Recent observations have revealed recruitment of the host GTPase Rab1 to the LCV by a process requiring the Dot/Icm system. Here, a visual screen was used to identify L. pneumophila mutants with defects in Rab1 recruitment. One of the factors identified in this screen was DrrA, a new Dot/Icm substrate protein translocated into host cells. We show that DrrA is a potent and highly specific Rab1 guanine nucleotide-exchange factor (GEF). DrrA can disrupt Rab1-mediated secretory transport to the Golgi apparatus by competing with endogenous exchange factors to recruit and activate Rab1 on plasma membrane-derived organelles. These data establish that intracellular pathogens have the capacity to directly modulate the activation state of a specific member of the Rab family of GTPases and thus further our understanding of the mechanisms used by bacterial pathogens to manipulate host vesicular transport.
- Subjects
LEGIONELLA pneumophila; INTRACELLULAR pathogens; LYSOSOMES; ENDOPLASMIC reticulum; BIOLOGICAL transport; BACTERIAL proteins; G proteins
- Publication
Nature Cell Biology, 2006, Vol 8, Issue 9, p971
- ISSN
1465-7392
- Publication type
Article
- DOI
10.1038/ncb1463