Proteomics

Dataset Information

0

Proteomics-based identification of DUBsubstrates using selective inhibitors

ABSTRACT: Deubiquitinating enzymes (DUBs) catalyze the removal of ubiquitin, thereby reversing the activity of E3 ubiquitin ligases and are central to the control of protein abundance and function. Despite the growing interest in DUBs as therapeutic targets, cellular functions for DUBs remain largely unknown and technical challenges often preclude the identification of DUB substrates in a comprehensive manner. Here we demonstrate that recently developed potent DUB inhibitors coupled to mass spectrometry-based proteomics can identify DUB substrates at a proteome-wide scale. We applied this methodology to USP7, a DUB widely investigated as a therapeutic target and identified novel substrates. We demonstrate that USP7 substrates are enriched for DNA repair enzymes and E3 ubiquitin ligases. This work provides not only a comprehensive annotation of USP7 substrates, but a general methodology widely applicable to other DUBs, which is critical for translational development of DUB targeted agents.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Eric Fischer  

LAB HEAD: Eric Fischer

PROVIDER: PXD020881 | Pride | 2021-04-06

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
esf_1123.raw Raw
esf_1124.raw Raw
esf_1125.raw Raw
esf_1126.raw Raw
esf_1127.raw Raw
Items per page:
1 - 5 of 25
altmetric image

Publications

Proteomics-Based Identification of DUB Substrates Using Selective Inhibitors.

Bushman Jonathan W JW   Donovan Katherine A KA   Schauer Nathan J NJ   Liu Xiaoxi X   Hu Wanyi W   Varca Anthony C AC   Buhrlage Sara J SJ   Fischer Eric S ES  

Cell chemical biology 20201001 1

Deubiquitinating enzymes (DUBs) catalyze the removal of ubiquitin, thereby reversing the activity of E3 ubiquitin ligases and are central to the control of protein abundance and function. Despite the growing interest in DUBs as therapeutic targets, cellular functions for DUBs remain largely unknown and technical challenges often preclude the identification of DUB substrates in a comprehensive manner. Here, we demonstrate that treatment with potent DUB inhibitors coupled to mass spectrometry-base  ...[more]

Similar Datasets

Proteomics Proteomics-based identification of DUBsubstrates using selective inhibitors
2021-01-18 | PXD020873 | Pride
Proteomics Proteomics-based identification of DUBsubstrates using selective inhibitors
2021-01-18 | PXD020882 | Pride
Proteomics Proteomics-based identification of DUBsubstrates using selective inhibitors
2021-01-18 | PXD020865 | Pride
Proteomics Unmasking functional redundancy of deubiquitylases enables specificity profiling and discovery of novel proteasome substrates
2022-09-02 | PXD016164 | Pride
Proteomics Proteomics of broad deubiquitylase inhibition unmasks redundant enzyme function to reveal substrates and assess enzyme specificity
2022-09-02 | PXD022762 | Pride
Proteomics Proteomics of broad deubiquitylase inhibition unmasks redundant enzyme function to reveal substrates and assess enzyme specificity
2021-09-09 | PXD022740 | Pride
Proteomics Substrate identification and specificity profiling of deubiquitylases against endogenously-generated ubiquitin-protein conjugates
2024-04-26 | PXD047866 | Pride
Transcriptomics Comprehensive landscape of active deubiquitinating enzymes profiled by advanced chemoproteomics
2019-08-31 | GSE134954 | GEO
Proteomics A proteomic approach for systematic mapping of human deubiquitinating enzymes substrates
2021-04-29 | PXD025443 | Pride
Proteomics USP7: combing tools towards selectivity
2019-03-13 | PXD012535 | Pride