{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dowen RH"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["15867-79"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2708883"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["284(23)"],"pubmed_abstract":["Bacterial phytopathogens employ a type III secretion system to deliver effector proteins into the plant cell to suppress defense pathways; however, the molecular mechanisms and subcellular localization strategies that drive effector function largely remain a mystery. Here, we demonstrate that the plant plasma membrane is the primary site for subcellular localization of the Pseudomonas syringae effector AvrPphB and five additional cysteine protease family members. AvrPphB and two AvrPphB-like effectors, ORF4 and NopT, autoproteolytically process following delivery into the plant cell to expose embedded sites for fatty acylation. Host-dependent lipidation of these three effectors directs plasma membrane localization and is required for the avirulence activity of AvrPphB. Surprisingly, the AvrPphB-like effectors RipT, HopC1, and HopN1 utilize an acylation-independent mechanism to localize to the cellular plasma membrane. Although some AvrPphB-like effectors employ acylation-independent localization strategies, others hijack the eukaryotic lipidation machinery to ensure plasma membrane localization, illustrating the diverse tactics employed by type III effectors to target specific subcellular compartments."],"journal":["The Journal of biological chemistry"],"pubmed_title":["A family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes."],"pmcid":["PMC2708883"],"funding_grant_id":["T32 GM007752","R01 AI060662","2 T32GM07752-25"],"pubmed_authors":["Shao F","Dowen RH","Ecker JR","Dixon JE","Engel JL"],"additional_accession":[]},"is_claimable":false,"name":"A family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes.","description":"Bacterial phytopathogens employ a type III secretion system to deliver effector proteins into the plant cell to suppress defense pathways; however, the molecular mechanisms and subcellular localization strategies that drive effector function largely remain a mystery. Here, we demonstrate that the plant plasma membrane is the primary site for subcellular localization of the Pseudomonas syringae effector AvrPphB and five additional cysteine protease family members. AvrPphB and two AvrPphB-like effectors, ORF4 and NopT, autoproteolytically process following delivery into the plant cell to expose embedded sites for fatty acylation. Host-dependent lipidation of these three effectors directs plasma membrane localization and is required for the avirulence activity of AvrPphB. Surprisingly, the AvrPphB-like effectors RipT, HopC1, and HopN1 utilize an acylation-independent mechanism to localize to the cellular plasma membrane. Although some AvrPphB-like effectors employ acylation-independent localization strategies, others hijack the eukaryotic lipidation machinery to ensure plasma membrane localization, illustrating the diverse tactics employed by type III effectors to target specific subcellular compartments.","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Jun","modification":"2020-11-22T09:10:37Z","creation":"2019-03-27T00:23:26Z"},"accession":"S-EPMC2708883","cross_references":{"pubmed":["19346252"],"doi":["10.1074/jbc.M900519200"]}}