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PXD021000-1

PXD021000 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe endosomal TbTpr86/TbUsp7/SkpZ (TUS) complex controls surface protein abundance in trypanosomes
DescriptionIn trypanosomes two deubiquitilating enzymes (DUBs), orthologous to human USP7 and VDU1, control abundance of a cohort of surface proteins, including invariant surface glycoproteins (ISGs). Silencing TbUsp7 partially inhibits endocytosis and invariant surface glycoprotein turnover. S-phase kinase-associated protein 1 (Skp1) has crucial roles in cell cycle progression, transcriptional regulation, signal transduction and other processes in animals and fungi by virtue of being a component of cullin E3 ubiquitin ligases. Unexpectedly, trypanosomes possess multiple Skp1 paralogs, including a divergent paralog designated SkpZ. SkpZ is implicated in suramin-sensitivity and endocytosis and decreases in abundance following TbUsp7 knockdown. SkpZ physically interacts with TbUsp7 and TbTpr86. The latter is a tetratricopeptide-repeat protein also implicated in suramin sensitivity and located close to the flagellar pocket/endosomes, consistent with a role in endocytosis. Further, silencing SkpZ reduced abundance of TbUsp7 and TbTpr86 and many trans-membrane domain surface proteins. Our data indicate that TbTpr, TbUsp7 and SkpZ form the ‘TUS’ complex that regulates abundance of a significant cohort of trypanosome surface proteins. 
HostingRepositoryPRIDE
AnnounceDate2025-01-08
AnnouncementXMLSubmission_2025-01-08_07:19:16.737.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterMartin Zoltner
SpeciesList scientific name: Trypanosoma brucei; NCBI TaxID: 5691;
ModificationListiodoacetamide derivatized residue
InstrumentLTQ Orbitrap Velos; Q Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-08-19 08:32:55ID requested
12025-01-08 07:19:17announced
Publication List
10.3389/FPARA.2023.1118284;
Keyword List
submitter keyword: ubiquitylation, Skp1,Trypanosoma brucei, surface proteome, TUS complex, cullin E3 ligase, USP7
Contact List
Mark C. Field
contact affiliationProfessor of Cell Biology and Parasitology
contact emailmfield@mac.com
lab head
Martin Zoltner
contact affiliationDivision of Biological Chemistry & Drug Discovery School of Life Sciences University of Dundee Dundee DD1 5EH
contact emailzoltnerm@natur.cuni.cz
dataset submitter
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Dataset FTP location
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