Profiling the Trypanosoma cruzi phosphoproteome
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da FIOCRUZ (ARCA) |
Texto Completo: | https://www.arca.fiocruz.br/handle/icict/40085 |
Resumo: | Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil. |
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Marchini, Fabrício KleryntonGodoy, Lyris Martins Franco deRampazzo, Rita de Cássia PontelloPavoni, Daniela ParadaProbst, Christian MacagnanGnad, FlorianMann, MatthiasKrieger, Marco Aurélio2020-02-19T14:39:34Z2020-02-19T14:39:34Z2011MARCHINI, Fabricio K. et al. Profiling the Trypanosoma cruzi Phosphoproteome. Plos One, v. 6, n. 9, p. 1-10, 2011.1932-6203https://www.arca.fiocruz.br/handle/icict/4008510.1371/journal.pone.00253811932-6203porPublic Library of ScienceTrypanosoma cruziKinetoplastidaPhosphorylationProtozoan ProteinsFosforilaciónProteínas ProtozoariasFosforilaçãoProteínas de ProtozoáriosProfiling the Trypanosoma cruzi phosphoproteomeinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleFundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil / Department of Proteomics and Signal Transduction. Max Planck Institute of Biochemistry. Martinsried, Germany.Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Department of Proteomics and Signal Transduction. Max Planck Institute of Biochemistry. Martinsried, Germany.Department of Proteomics and Signal Transduction. Max Planck Institute of Biochemistry. Martinsried, Germany.Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.Protein phosphorylation is a reversible post-translational modification essential for the regulation of several signal transduction pathways and biological processes in the living cell. Therefore, the identification of protein phosphorylation sites is crucial to understand cell signaling control at the molecular level. Based on mass spectrometry, recent studies have reported the large-scale mapping of phosphorylation sites in various eukaryotes and prokaryotes. However, little is known about the impact of phosphorylation in protozoan parasites. To in depth characterize the phosphoproteome of Trypanosoma cruzi, a parasite of the Kinetoplastida class, protein samples from cells at different phases of the metacyclogenesis--differentiation process of the parasites from non-infective epimastigotes to infective metacyclic trypomastigotes--were enriched for phosphopeptides using TiO(2) chromatography and analyzed on an LTQ-Orbitrap mass spectrometer. In total, 1,671 proteins were identified, including 753 phosphoproteins, containing a total of 2,572 phosphorylation sites. The distribution of phosphorylated residues was 2,162 (84.1%) on serine, 384 (14.9%) on threonine and 26 (1.0%) on tyrosine. Here, we also report several consensus phosphorylation sequence motifs and as some of these conserved groups have enriched biological functions, we can infer the regulation by protein kinases of this functions. To our knowledge, our phosphoproteome is the most comprehensive dataset identified until now for Kinetoplastida species. Here we also were able to extract biological information and infer groups of sites phosphorylated by the same protein kinase. To make our data accessible to the scientific community, we uploaded our study to the data repositories PHOSIDA, Proteome Commons and TriTrypDB enabling researchers to access information about the phosphorylation sites identified here.info:eu-repo/semantics/openAccessreponame:Repositório Institucional da FIOCRUZ (ARCA)instname:Fundação Oswaldo Cruz (FIOCRUZ)instacron:FIOCRUZLICENSElicense.txtlicense.txttext/plain; charset=utf-83084https://www.arca.fiocruz.br/bitstream/icict/40085/1/license.txt783568c2893d2e25a99990b126be1772MD51ORIGINALjournal.pone.002538ok.PDFjournal.pone.002538ok.PDFapplication/pdf411332https://www.arca.fiocruz.br/bitstream/icict/40085/2/journal.pone.002538ok.PDF1c64dda8f58ad34d9bd06e475d53ef4aMD52TEXTjournal.pone.002538ok.PDF.txtjournal.pone.002538ok.PDF.txtExtracted texttext/plain55275https://www.arca.fiocruz.br/bitstream/icict/40085/3/journal.pone.002538ok.PDF.txta785af0b6edfdb3fef865e2c2d6efdacMD53icict/400852020-02-20 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dc.title.pt_BR.fl_str_mv |
Profiling the Trypanosoma cruzi phosphoproteome |
title |
Profiling the Trypanosoma cruzi phosphoproteome |
spellingShingle |
Profiling the Trypanosoma cruzi phosphoproteome Marchini, Fabrício Klerynton Trypanosoma cruzi Kinetoplastida Phosphorylation Protozoan Proteins Fosforilación Proteínas Protozoarias Fosforilação Proteínas de Protozoários |
title_short |
Profiling the Trypanosoma cruzi phosphoproteome |
title_full |
Profiling the Trypanosoma cruzi phosphoproteome |
title_fullStr |
Profiling the Trypanosoma cruzi phosphoproteome |
title_full_unstemmed |
Profiling the Trypanosoma cruzi phosphoproteome |
title_sort |
Profiling the Trypanosoma cruzi phosphoproteome |
author |
Marchini, Fabrício Klerynton |
author_facet |
Marchini, Fabrício Klerynton Godoy, Lyris Martins Franco de Rampazzo, Rita de Cássia Pontello Pavoni, Daniela Parada Probst, Christian Macagnan Gnad, Florian Mann, Matthias Krieger, Marco Aurélio |
author_role |
author |
author2 |
Godoy, Lyris Martins Franco de Rampazzo, Rita de Cássia Pontello Pavoni, Daniela Parada Probst, Christian Macagnan Gnad, Florian Mann, Matthias Krieger, Marco Aurélio |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Marchini, Fabrício Klerynton Godoy, Lyris Martins Franco de Rampazzo, Rita de Cássia Pontello Pavoni, Daniela Parada Probst, Christian Macagnan Gnad, Florian Mann, Matthias Krieger, Marco Aurélio |
dc.subject.other.pt_BR.fl_str_mv |
Trypanosoma cruzi Kinetoplastida |
topic |
Trypanosoma cruzi Kinetoplastida Phosphorylation Protozoan Proteins Fosforilación Proteínas Protozoarias Fosforilação Proteínas de Protozoários |
dc.subject.en.pt_BR.fl_str_mv |
Phosphorylation Protozoan Proteins |
dc.subject.es.pt_BR.fl_str_mv |
Fosforilación Proteínas Protozoarias |
dc.subject.decs.pt_BR.fl_str_mv |
Fosforilação Proteínas de Protozoários |
description |
Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil. |
publishDate |
2011 |
dc.date.issued.fl_str_mv |
2011 |
dc.date.accessioned.fl_str_mv |
2020-02-19T14:39:34Z |
dc.date.available.fl_str_mv |
2020-02-19T14:39:34Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
MARCHINI, Fabricio K. et al. Profiling the Trypanosoma cruzi Phosphoproteome. Plos One, v. 6, n. 9, p. 1-10, 2011. |
dc.identifier.uri.fl_str_mv |
https://www.arca.fiocruz.br/handle/icict/40085 |
dc.identifier.issn.pt_BR.fl_str_mv |
1932-6203 |
dc.identifier.doi.none.fl_str_mv |
10.1371/journal.pone.0025381 |
dc.identifier.eissn.none.fl_str_mv |
1932-6203 |
identifier_str_mv |
MARCHINI, Fabricio K. et al. Profiling the Trypanosoma cruzi Phosphoproteome. Plos One, v. 6, n. 9, p. 1-10, 2011. 1932-6203 10.1371/journal.pone.0025381 |
url |
https://www.arca.fiocruz.br/handle/icict/40085 |
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por |
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por |
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info:eu-repo/semantics/openAccess |
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openAccess |
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Public Library of Science |
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Public Library of Science |
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