Global analysis of palmitoylated proteins in Toxoplasma gondii
Supporting Files
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Oct 14 2015
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Details
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Alternative Title:Cell Host Microbe
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Personal Author:
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Description: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.
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Subjects:
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Source:Cell Host Microbe. 18(4):501-511.
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Pubmed ID:26468752
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Pubmed Central ID:PMC4694575
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Document Type:
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Funding:5T32AI007328/AI/NIAID NIH HHS/United States ; R00CA151460/CA/NCI NIH HHS/United States ; R01 AI105191/AI/NIAID NIH HHS/United States ; R01 GM111703/GM/NIGMS NIH HHS/United States ; T32 AI007328/AI/NIAID NIH HHS/United States ; DP2GM114848/DP/NCCDPHP CDC HHS/United States ; R01GM111703/GM/NIGMS NIH HHS/United States ; DP2 GM114848/GM/NIGMS NIH HHS/United States ; R00 CA151460/CA/NCI NIH HHS/United States ; R01AI063276/AI/NIAID NIH HHS/United States ; R01 AI063276/AI/NIAID NIH HHS/United States
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Volume:18
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Issue:4
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Collection(s):
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Main Document Checksum:urn:sha256:b2542ffa7be1203d85fbb7a46321f81bb13dfd1db79015bff608fe2beea91a7b
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Supporting Files
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