期刊
NATURE CELL BIOLOGY
卷 8, 期 9, 页码 971-U76出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1463
关键词
-
类别
资金
- NIAID NIH HHS [R01 AI041699, AI41699, R01 AI041699-10] Funding Source: Medline
- NIGMS NIH HHS [GM56324] Funding Source: Medline
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(1,2). 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(3-7). Recent observations have revealed recruitment of the host GTPase Rab1 to the LCV by a process requiring the Dot/Icm system(8,9). 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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据