GPMDB00423OtherJones ML, et al.InstrumentNot AvailableNot availableHuman, Plasmodium_falciparum_refseq22901544Not availableMalaria Programme, The Wellcome Trust Sanger Institutehttp://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004610http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004611http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004615http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004612http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004613http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004618http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004619http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004616http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM11210004617CL:0000232 erythrocyteGPMDBAsexual stage Plasmodium falciparum replicates and undergoes a tightly regulated developmental process in human erythrocytes. One mechanism involved in the regulation of this process is posttranslational modification (PTM) of parasite proteins. Palmitoylation is a PTM in which cysteine residues undergo a reversible lipid modification, which can regulate target proteins in diverse ways. Using complementary palmitoyl protein purification approaches and quantitative mass spectrometry, we examined protein palmitoylation in asexual-stage P. falciparum parasites and identified over 400 palmitoylated proteins, including those involved in cytoadherence, drug resistance, signaling, development, and invasion. Consistent with the prevalence of palmitoylated proteins, palmitoylation is essential for P. falciparum asexual development and influences erythrocyte invasion by directly regulating the stability of components of the actin-myosin invasion motor. Furthermore, P. falciparum uses palmitoylation in diverse ways, stably modifying some proteins while dynamically palmitoylating others. Palmitoylation therefore plays a central role in regulating P. falciparum blood stage development.Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis.Jones Matthew L ML,Collins Mark O MO,Goulding David D,Choudhary Jyoti S JS,Rayner Julian C JC,Jones Matthew L ML, Collins Mark O MO, Goulding David D, Choudhary Jyoti S JS, Rayner Julian C JCConcept, development, Role Concept, single-organism developmental process, determination, Roles, Plasmodiums, chemical analysis, protein amino acid palmitoylation, Role Concepts, Role, Concepts, assay, virulence.Mass Spectrum Analysis, close to, Mass Spectrum, host organism, data, biological signaling, Analyses, cell, single-organism developmental process., protein amino acid palmitoylation, developmental stage, Proteins, drug susceptibility/resistance, number, Spectrometry, Gene, proteins, Spectrum Analyses, presence, Spectrum Analysis, Cell, signalling, Protein Gene Products, Drug, near to, Spectroscopy, polypeptide, Gene Proteins, development, count in organism, count, Parasite, signalling process, approaches, signaling process, vicinity of, Protein, Mass, Gene Products, Resistance, stage, quantitative, Analysis, drug resistance, Mass Spectrum Analyses, Mass Spectroscopy, single organism signaling, presence or absence in organismConcept, development, Role Concept, single-organism developmental process, determination, Roles, Plasmodiums, chemical analysis, protein amino acid palmitoylation, Role Concepts, Role, Concepts, assay, virulence.projections, biological signaling, posttranslational modification, human being, Cysteine Hydrochloride, single-organism developmental process, DFNA4A, lamellae, single-organism developmental process., Blood, developmental stage, drug susceptibility/resistance, number, L-Zystein, RBC, Gene, Spectrum Analyses, Homo sapiense, L-cysteine, process of organ, presence, protrusion, lamella, Homo spaiens, MYH17, Homo sapien, Roles, Homo sapians, Gene Products, Mass, Concepts, Half-Cystine, Analysis, Blood Corpuscle, drug resistance, Mass Spectroscopy, palmitoylation, Mass Spectrum Analysis, portion of blood, C, posttranslational amino acid modification, Homo sapients, Red Blood, Analyses, Prevalences, red blood corpuscle, L Cysteine, proteins, ridges, posttranslational protein modification, man, circulating cells, myosin, Homo sapience, CYSTEINE, Homo sampiens, papilla, signaling process, falciparums, Role Concepts, Red, FREE CYSTEINE, MHC16, stage, C3H7NO2S, Half Cystine, (2R)-2-amino-3-mercaptopropanoic acid, Plasmodium falciparums, laminae, Home sapiens, single organism signaling, close to, anatomical protrusion, whole blood, Zinc Cysteinate, vertebrate blood, anatomical process, NMHC-II-C, Proteins, Plasmodium, lamina, flanges, Red Blood Cell, Cys, Spectrum Analysis, Concept, near to, Spectroscopy, development, polypeptide, count in organism, Role Concept, count, blood cells, Homo sapian, Protein, shelf, Resistance, Role, Corpuscles, NMHC II-C, Red Blood Corpuscle, Homo sapeins, (2R)-2-amino-3-sulfanylpropanoic acid, flange, Mass Spectrum Analyses, organ process, DFNA4, Blood Cells, Mass Spectrum, Blood Cell, PNMHH, Palmitoylation, PTM, Peripheral Blood, Plasmodium (Laverania) falciparum, shelves, protein amino acid palmitoylation, red blood cell, Spectrometry, Humo sapiens, L-2-Amino-3-mercaptopropionic acid, L-Cysteine, (R)-2-amino-3-mercaptopropanoic acid, circulating cell, Homo sapines, projection, ridge, human, post-translational amino acid modification, L-Cystein, signalling, Protein Gene Products, Drug, Reticuloendothelial System, process, processes, Gene Proteins, Red Blood Corpuscles, Corpuscle, Homo spiens, "human" EXACT genbank_common_name [], Parasite, signalling process, Red Blood Cells, spine, post-translational modification, approaches, vicinity of, Erythrocyte, processus, E920, regulation, Blood Corpuscles, quantitative, malaria parasite P. falciparum, presence or absence in 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Reanalysis0.00.00.0129549660703269580.01.0falseAnalysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis.PRIDE ID: 17889. Data published as part of Cell Host Microbe. 2012 Aug 16;12(2):246-58 [[http://www.ncbi.nlm.nih.gov/pubmed/22901544 PubMed]]. From the Abstract: {{i}} ... sing complementary palmitoyl protein purification approaches and quantitative mass spectrometry, we examined protein palmitoylation in asexual-stage P. falciparum parasites and identified over 400 palmitoylated proteins, including those involved in cytoadherence, drug resistance, signaling, development, and invasion ...{{/i}}2012-09-29GPM1121000461122901544