A milestone for biomedical research
Mass spectrometry-based draft of the mouse proteome
The laboratory mouse ranks among the most important experimental systems for biomedical research and molecular reference maps of such models are essential informational tools. “We present a quantitative draft of the mouse proteome and phosphoproteome constructed from 41 healthy tissues. These molecules are cellular regulators of normal as well as pathological processes," says Bernhard Küster, Professor of Proteomics and Bioanalytics.
The researchers now show in a Nature Methods publication what insights can be gleaned from the data. For instance, tissue- and cell-type resolved profiles provide protein evidence for the expression of 17,000 genes and thousands of isoforms, proteins that arise from the same gene but differ in structure.
Furthermore, 50,000 phosphorylation sites could be found. These are specific and particularly important parts of proteins that regulate processes in the cell. In other words, the research work provides information about how many of the approximately 20,000 mouse genes exist as proteins, where they are expressed, in what quantities they occur and how active they are.
Proteogenomic comparison of mouse, human and Arabidopsis reveal common and distinct mechanisms of gene expression regulation and, despite many similarities, numerous differentially abundant orthologs that likely serve species-specific functions. "We leverage the mouse proteome by integrating more than 400 phenotypic drug and radiation response data sets with the proteomes of 66 pancreatic ductal adenocarcinoma (PDAC) cell lines to reveal molecular markers for drug sensitivity and resistance," says Piero Giansanti, Ph.D., first author of the study.
Giansanti, P., Samaras, P., Bian, Y. et al.: Mass spectrometry-based draft of the mouse proteome. Nat Methods (2022). doi.org/10.1038/s41592-022-01526-y
This work was supported by:
- Deutsche Forschungsgemeinschaft (German Research Foundation)
- Bundesministerium für Bildung und Forschung (Federal Ministry of Education and Research)
- EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council)
Contacts to this article:
Prof. Dr. Bernhard Küster
Technical University of Munich
Chair of Proteomics and Bioanalytics
TUM School of Life Sciences