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- W2002375189 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." @default.
- W2002375189 created "2016-06-24" @default.
- W2002375189 creator A5013385995 @default.
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- W2002375189 date "2009-06-01" @default.
- W2002375189 modified "2023-10-16" @default.
- W2002375189 title "A Family of Bacterial Cysteine Protease Type III Effectors Utilizes Acylation-dependent and -independent Strategies to Localize to Plasma Membranes" @default.
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- W2002375189 doi "https://doi.org/10.1074/jbc.m900519200" @default.
- W2002375189 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2708883" @default.
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