PXD027712 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | A proteomic study on the membrane protein fraction of T cells confirms high substrate selectivity for the ER translocation inhibitor cyclotriazadisulfonamide |
Description | Cyclotriazadisulfonamide (CADA) inhibits the co-translational translocation of type I integral membrane protein human CD4 (huCD4) across the ER in a signal peptide (SP)-dependent way. Previously, sortilin was identified as a secondary substrate for CADA but showed reduced CADA sensitivity as compared to huCD4. We performed a quantitative proteomic study on the membrane fraction of human T-cells to analyze how many integral membrane proteins are sensitive to CADA. We employed stable isotope labelling by amino acids in cell culture (SILAC) technique in combination with quantitative mass spectrometry on CADA-treated human T-lymphoid SUP-T1 cells expressing high levels of huCD4. In line with our previous reports, our current proteomic analysis demonstrated that only a very small subset of proteins is depleted by CADA. Our data also confirmed that cellular expression of both huCD4 and sortilin are affected by CADA-treatment of SUP-T1 cells. Furthermore, three additional targets for CADA are identified, namely, Endoplasmic Reticulum Lectin 1 (ERLEC1), Inactive Tyrosine-Protein Kinase 7 (PTK7), and DnaJ Homolog Subfamily C member 3 (DNAJC3). The sensitivity of these proteins for the translocation inhibitor CADA was confirmed by biochemical experiments including Western blots, flow cytometry and cell free in vitro translation/translocation experiments. |
HostingRepository | PRIDE |
AnnounceDate | 2021-09-08 |
AnnouncementXML | Submission_2021-09-08_06:27:49.919.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Fan Liu |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-08-05 05:44:28 | ID requested | |
⏵ 1 | 2021-09-08 06:27:50 | announced | |
Publication List
Pauwels E, Rutz C, Provinciael B, Stroobants J, Schols D, Hartmann E, Krause E, Stephanowitz H, Sch, ü, lein R, Vermeire K, A Proteomic Study on the Membrane Protein Fraction of T Cells Confirms High Substrate Selectivity for the ER Translocation Inhibitor Cyclotriazadisulfonamide. Mol Cell Proteomics, 20():100144(2021) [pubmed] |
Keyword List
submitter keyword: CD4 |
cyclotriazadisulfonamide (CADA) |
ER co-translational translocation |
signal peptide |
SILAC |
Contact List
Fan Liu |
contact affiliation | Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) |
contact email | fliu@fmp-berlin.de |
lab head | |
Fan Liu |
contact affiliation | Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) |
contact email | fliu@fmp-berlin.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD027712
- Label: PRIDE project
- Name: A proteomic study on the membrane protein fraction of T cells confirms high substrate selectivity for the ER translocation inhibitor cyclotriazadisulfonamide