title: Priming and activation of NADPH oxidases in plants and animals.
abstract: In mammals, engagement of Toll-like receptors by microbe-associated molecular patterns enhances the responsiveness of NADPH oxidases. Two recent papers report a similar 'priming' mechanism for the plant oxidase RbohD. Despite lacking structural homology, the functional parallels between plants and animals reveal that a common regulatory logic arose by convergent evolution.
authors.affiliation: Program in Cell Biology, Hospital for Sick Children, 686 Bay Street, Toronto, Ontario, M5G 0A4.
authors.forename: Johnathan
authors.initials: J
authors.lastname: Canton
authors.affiliation: Program in Cell Biology, Hospital for Sick Children, 686 Bay Street, Toronto, Ontario, M5G 0A4; Keenan Research Centre of the Li Ka Shing Knowledge Institute, St. Michael's Hospital, 290 Victoria Street, Toronto, Ontario, M5C 1N8 Canada. Electronic address: sergio.grinstein@sickkids.ca.
authors.forename: Sergio
authors.initials: S
authors.lastname: Grinstein
mesh_terms: D000818:Animals; D005075:Biological Evolution; D004789:Enzyme Activation; D006801:Humans; D019255:NADPH Oxidases / Q000276:immunology*; D010940:Plant Proteins / Q000276:immunology*; D010944:Plants; D017382:Reactive Oxygen Species / Q000378:metabolism; D040681:Structural Homology, Protein; D051193:Toll-Like Receptors / Q000378:metabolism*
chemical_list: D010940:Plant Proteins; D017382:Reactive Oxygen Species; D051193:Toll-Like Receptors; D019255:NADPH Oxidases
keywords: NADPH oxidase; NOX; PAMP; ROS; RbohD; TLR; pattern recognition receptor; priming; reactive oxygen species