MassIVE MSV000093577

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Analysis of p53 independent functions of the Mdm2 MdmX complex using data independent acquisition based profiling

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Description

We utilized data independent acquisition (DIA) to study the poorly understood biology of Mdm2 and MdmX in a p53 null context. Mdm2 and MdmX form a E3 ligase complex that has as its most well studied function the negative regulation of the tumor suppressor p53, however, it is also known to interact with many other proteins in a p53 independent manner. In this work, small molecule and siRNA-based technology were used to modify Mdm2/Mdmx activity in a human non small cell lung carcinoma cell line lacking p53 expression. Study of the proteome of these cells helped identify biological processes where Mdm2 and MdmX may be playing role in a p53 independent manner. Proteins from H1299 cells, treated with the drug MEL23, siRNA against Mdm2 or MdmX were analyzed. Protein ontology and function were analyzed demonstrating which pathways are affected by modulation of the proteins that originate the complex. Insights on how those functions are dependent on the activity of the complex could also be proposed based on comparison among the three groups of samples. We selected a potential target from the DIA analysis and validated it by immunoblotting and qPCR demonstrating a new interaction partner of the Mdm2 MdmX complex in human cells. [doi:10.25345/C5251FW65] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: cancer ; data independent acquisition ; label-free proteomics ; Mdm2 ; MdmX ; p53 independent functions

Contact

Principal Investigators:
(in alphabetical order) 		Carol Prives, Columbia University, United States
Lewis M. Brown, Columbia University, United States
Submitting User: cuproteomics
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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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