{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang Z"],"funding":["NIAID NIH HHS"],"pagination":["53"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6175885"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4"],"pubmed_abstract":["Posttranslational modification of key host proteins by virulence factors is an important theme in bacterial pathogenesis. A remarkable example is the reversible modifications of the small GTPase Rab1 by multiple effectors of the bacterial pathogen <i>Legionella pneumophila</i>. Previous studies have shown that the effector SetA, dependent on a functional glucosyltransferase domain, interferes with host secretory pathways. However, the enzymatic substrate(s) of SetA in host cells remains unknown. Here, by using cross-linking mass spectrometry we uncovered Rab1 as the target of SetA during <i>L. pneumophila</i> infection. Biochemical studies establish that SetA covalently attaches a glucose moiety to Thr<sub>75</sub> within the switch II region of Rab1, inhibiting its intrinsic GTPase activi"],"journal":["Cell discovery"],"pubmed_title":["Regulation of the small GTPase Rab1 function by a bacterial glucosyltransferase."],"pmcid":["PMC6175885"],"funding_grant_id":["R01 AI127465"],"pubmed_authors":["McCloskey A","Cheng S","Liu X","Liu Y","Wu M","Xue C","Luo ZQ","Fu J","Yu Z","Wang Z"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of the small GTPase Rab1 function by a bacterial glucosyltransferase.","description":"Posttranslational modification of key host proteins by virulence factors is an important theme in bacterial pathogenesis. A remarkable example is the reversible modifications of the small GTPase Rab1 by multiple effectors of the bacterial pathogen <i>Legionella pneumophila</i>. Previous studies have shown that the effector SetA, dependent on a functional glucosyltransferase domain, interferes with host secretory pathways. However, the enzymatic substrate(s) of SetA in host cells remains unknown. Here, by using cross-linking mass spectrometry we uncovered Rab1 as the target of SetA during <i>L. pneumophila</i> infection. Biochemical studies establish that SetA covalently attaches a glucose moiety to Thr<sub>75</sub> within the switch II region of Rab1, inhibiting its intrinsic GTPase activi","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018","modification":"2025-04-21T21:52:42.799Z","creation":"2019-03-27T00:02:41Z"},"accession":"S-EPMC6175885","cross_references":{"pubmed":["30323948"],"doi":["10.1038/s41421-018-0055-9"]}}