Publication Date:
2011-07-08
Description:
Legionella pneumophila actively modulates host vesicle trafficking pathways to facilitate its intracellular replication with effectors translocated by the Dot/Icm type IV secretion system (T4SS). The SidM/DrrA protein functions by locking the small GTPase Rab1 into an active form by its guanine nucleotide exchange factor (GEF) and AMPylation activity. Here we demonstrate that the L. pneumophila protein SidD preferably deAMPylates Rab1. We found that the deAMPylation activity of SidD could suppress the toxicity of SidM to yeast and is required to release Rab1 from bacterial phagosomes efficiently. A molecular mechanism for the temporal control of Rab1 activity in different phases of L. pneumophila infection is thus established. These observations indicate that AMPylation-mediated signal transduction is a reversible process regulated by specific enzymes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3146296/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3146296/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tan, Yunhao -- Luo, Zhao-Qing -- K02 AI085403/AI/NIAID NIH HHS/ -- K02 AI085403-02/AI/NIAID NIH HHS/ -- K02AI085403/AI/NIAID NIH HHS/ -- R01 AI069344/AI/NIAID NIH HHS/ -- R01 AI069344-05/AI/NIAID NIH HHS/ -- R01AI069344/AI/NIAID NIH HHS/ -- R21 AI092043/AI/NIAID NIH HHS/ -- R21 AI092043-01/AI/NIAID NIH HHS/ -- R21AI092043/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Jul 6;475(7357):506-9. doi: 10.1038/nature10307.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21734656" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Aspartic Acid/chemistry
;
Bacterial Proteins/chemistry/genetics/*metabolism/toxicity
;
Cells, Cultured
;
Female
;
Guanine Nucleotide Exchange Factors/genetics/metabolism/toxicity
;
Legionella pneumophila/*enzymology
;
Legionnaires' Disease/*enzymology/physiopathology
;
Macrophages/enzymology/pathology
;
Mice
;
Phenotype
;
Plasmids/genetics
;
Saccharomyces cerevisiae/genetics/growth & development/metabolism
;
Time Factors
;
Transformation, Genetic
;
rab1 GTP-Binding Proteins/*metabolism
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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