VCP–adaptor interactions are exceptionally dynamic and subject to differential modulation by a VCP inhibitor
In this study we use a combination of mass spectrometry-based proteomics and biophysical studies to characterize the interaction of adaptors with VCP. Our results reveal that most VCP–adaptor interactions are characterized by exceptionally rapid dynamics that in some cases are modulated by the VCP inhibitor NMS873. These findings have significant implications for both the regulation of VCP function and the impact of VCP inhibition on different VCP–adaptor complexes.
Sample Processing Protocol
Cell culture, VCP inhibitor vs Control. Several types of proteomics workflows were applied. 1) Size exclusion fractionation, data dependent MS/MS. 2) Crosslinking with DSP, cell lysis, AP-MS, data dependent MS/MS.
Data Processing Protocol
Maxquant 18.104.22.168 for database search and quantification including SILAC and Label-free. Various tool for data interpretation, such as DAVIS, R scripts.
Corresponding dataset(s) in other omics resources
Dataset visualisation in external resources
Xue L, Blythe EE, Freiberger EC, Mamrosh J, Hebert AS, Reitsma JM, Hess S, Coon JJ, Deshaies RJ. VCP-adaptor interactions are exceptionally dynamic and subject to differential modulation by a VCP inhibitor. Mol Cell Proteomics. 2016 Jul 12. pii: mcp.M116.061036 PubMed: 27406709