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PXD018761

PXD018761 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleProteome changes upon modulation of eIF2α phosphorylation in Trypanosoma cruzi epimastigotes
DescriptionTrypanosomatids regulate gene expression mainly at the post-transcriptional level through processing, exporting and stabilizing mRNA and control of translation. In most eukaryotes, protein synthesis is regulated by phosphorylation of eukaryotic initiation factor 2 (eIF2) at serine 51. Phosphorylation halts overall translation by decreasing availability of initiator tRNAmet to form translating ribosomes. In trypanosomatids the N-terminus of eIF2α is extended with threonine 169 the homologous phosphorylated residue and eIF2α phosphorylation increases in proliferative intracellular forms prior to differentiation into trypomastigotes. Here we analyse the proteome changes in epimatigotes upon eIF2αT169A mutation and knock-out of the kinase TcK11, an ortolog of the general control nonderepressible 2 (GCN2)kinases which have been implicated in eukaryotic eIF2α ser51 phosphorylation.
HostingRepositoryPRIDE
AnnounceDate2020-07-06
AnnouncementXMLSubmission_2020-07-06_07:55:02.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterMartin Zoltner
SpeciesList scientific name: Trypanosoma cruzi; NCBI TaxID: 5693;
ModificationListiodoacetamide derivatized residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-04-23 05:27:41ID requested
12020-07-06 07:55:03announced
Publication List
Castro Machado F, Bittencourt-Cunha P, Malvezzi AM, Arico M, Radio S, Smircich P, Zoltner M, Field MC, Schenkman S, phosphorylation is regulated in intracellular amastigotes for the generation of infective Trypanosoma cruzi trypomastigote forms. Cell Microbiol, 22(11):e13243(2020) [pubmed]
Keyword List
submitter keyword: Trypanosoma cruzi, translation, differentiation, virulence, phosphorylation, eIF2
Contact List
Sergio Schenkman
contact affiliationDepartmento de Microbiologia, Imunologia e Parasitologia, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, SP, Brazil
contact emailsschenkman@unifesp.br
lab head
Martin Zoltner
contact affiliationDivision of Biological Chemistry & Drug Discovery School of Life Sciences University of Dundee Dundee DD1 5EH
contact emailm.zoltner@dundee.ac.uk
dataset submitter
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Dataset FTP location
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