PXD004941 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Integrative analysis of proteome and ubiquitylome reveals unique features of protein ubiquitylation and mitochondria in gefitinib resistant non-small cell lung cancer cells |
Description | Even though gefitinib, a tyrosine kinase inhibitor, widely used in treating non-small cell lung cancer (NSCLC) patients carrying EGFR activating mutations, most patients will develop gefitinib resistance. Protein ubiquitylation is one of major posttranslational modifications affecting the stability or function of the protein. However, the role of protein ubiquitylation in gefitinib resistance is poorly understood. To systematically identify the global change in protein ubiquitylation during gefitinib resistance, we carried out quantitative global proteome and ubiquitylome study by using cells with stable isotopic labeling with amino acid in cell culture (SILAC) followed by affinity enrichment of ubiquitylated peptides and subsequent liquid chromatography–tandem mass spectrometry (LC-MS/MS) analysis. Our study quantified are differentially regulated in ubiquitylation between gefitinib resistant and sensitive cells. Among them, 799 lysine sites were up-regulated in ubiquitylation in resistant cells, which are enriched in pathways, such as SNARE interaction in vesicle transport, endocytosis, phagosome, and lysosome, etc. In addition, we also found cells. The proteins carry these sites are involved in pathways including metabolic pathways, gap junction, and biosynthesis of amino acids, etc, This data indicate that gefitinib resistance dramatically alters the landscape of ubiquitylation in the cells. Furthermore, by integrating the genome-wide transcriptome data, we discovered that complexes I and IV in the electron transport chain of the mitochondria are up-regulated, while complexes II and III are down-regulated in resistant cells. Overall, these results reveal the unique features of ubiquitylation and mitochondria during gefitinib resistance, which will help to a better understanding of the role(s) of ubiquitylation, and to identify new therapeutic targets in overcoming gefitinib resistance. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:32:35.076.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | zhu taotao |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | ubiquitination signature dipeptidyl lysine |
Instrument | LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2016-09-12 03:59:11 | ID requested | |
1 | 2018-07-05 04:52:46 | announced | |
⏵ 2 | 2024-10-22 04:32:37 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1002/pmic.201700388; |
Li W, Wang H, Yang Y, Zhao T, Zhang Z, Tian Y, Shi Z, Peng X, Li F, Feng Y, Zhang L, Jiang G, Zhang F, Integrative Analysis of Proteome and Ubiquitylome Reveals Unique Features of Lysosomal and Endocytic Pathways in Gefitinib-Resistant Non-Small Cell Lung Cancer Cells. Proteomics, 18(15):e1700388(2018) [pubmed] |
Keyword List
curator keyword: Biomedical |
submitter keyword: Human, LC_MSMS, lung, non-small cell lung cancer cells |
Contact List
Zhang Fan |
contact affiliation | Department of Thoracic Surgery, Shanghai Pulmonary Hospital, Tongji University School of 6 Medicine, 507 Zhengmin Road, Shanghai 200433, China |
contact email | fzhang@tongji.edu.cn |
lab head | |
zhu taotao |
contact affiliation | PTM biolab (Hangzhou) |
contact email | taotao_zhu@ptm-biolab.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD004941
- Label: PRIDE project
- Name: Integrative analysis of proteome and ubiquitylome reveals unique features of protein ubiquitylation and mitochondria in gefitinib resistant non-small cell lung cancer cells