title: Global Analysis of Palmitoylated Proteins in Toxoplasma gondii.
abstract: Post-translational modifications (PTMs) such as palmitoylation are critical for the lytic cycle of the protozoan parasite Toxoplasma gondii. While palmitoylation is involved in invasion, motility, and cell morphology, the proteins that utilize this PTM remain largely unknown. Using a chemical proteomic approach, we report a comprehensive analysis of palmitoylated proteins in T. gondii, identifying a total of 282 proteins, including cytosolic, membrane-associated, and transmembrane proteins. From this large set of palmitoylated targets, we validate palmitoylation of proteins involved in motility (myosin light chain 1, myosin A), cell morphology (PhIL1), and host cell invasion (apical membrane antigen 1, AMA1). Further studies reveal that blocking AMA1 palmitoylation enhances the release of AMA1 and other invasion-related proteins from apical secretory organelles, suggesting a previously unrecognized role for AMA1. These findings suggest that palmitoylation is ubiquitous throughout the T. gondii proteome and reveal insights into the biology of this important human pathogen.
authors.affiliation: Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors.forename: Ian T
authors.initials: IT
authors.lastname: Foe
authors.affiliation: Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors.forename: Matthew A
authors.initials: MA
authors.lastname: Child
authors.affiliation: Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
authors.forename: Jaimeen D
authors.initials: JD
authors.lastname: Majmudar
authors.affiliation: Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
authors.forename: Shruthi
authors.initials: S
authors.lastname: Krishnamurthy
authors.affiliation: Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors.forename: Wouter A
authors.initials: WA
authors.lastname: van der Linden
authors.affiliation: Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
authors.forename: Gary E
authors.initials: GE
authors.lastname: Ward
authors.affiliation: Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: brentrm@umich.edu.
authors.forename: Brent R
authors.initials: BR
authors.lastname: Martin
authors.affiliation: Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: mbogyo@stanford.edu.
authors.forename: Matthew
authors.initials: M
authors.lastname: Bogyo
mesh_terms: D004705:Endocytosis; D006801:Humans; D008124:Locomotion; D010169:Palmitic Acids / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000032:analysis* / Q000378:metabolism*; D020543:Proteome / Q000032:analysis*; D014122:Toxoplasma / Q000737:chemistry* / Q000166:cytology / Q000502:physiology; D014774:Virulence
chemical_list: D010169:Palmitic Acids; D011506:Proteins; D020543:Proteome