期刊
MOLECULAR SYSTEMS BIOLOGY
卷 11, 期 1, 页码 -出版社
WILEY
DOI: 10.15252/msb.20145497
关键词
affinity purification; correlation profiling; label-free quantitative proteomics; mass spectrometry
资金
- ARC (Association pour la Recherche sur le Cancer) foundation
- Region Midi-Pyrenees
- European funds (Fonds Europeens de Developpement Regional, FEDER)
- Toulouse Metropole
- French Ministry of Research
- Investissement d'Avenir Infrastructures Nationales en Biologie et Sante program (ProFI) [ANR-10-INBS-08]
In eukaryotic cells, intracellular protein breakdown is mainly performed by the ubiquitin-proteasome system. Proteasomes are supramolecular protein complexes formed by the association of multiple sub-complexes and interacting proteins. Therefore, they exhibit a very high heterogeneity whose function is still not well understood. Here, using a newly developed method based on the combination of affinity purification and protein correlation profiling associated with high-resolution mass spectrometry, we comprehensively characterized proteasome heterogeneity and identified previously unknown preferential associations within proteasome sub-complexes. In particular, we showed for the first time that the two main proteasome subtypes, standard proteasome and immunoproteasome, interact with a different subset of important regulators. This trend was observed in very diverse human cell types and was confirmed by changing the relative proportions of both 20S proteasome forms using interferon-. The new method developed here constitutes an innovative and powerful strategy that could be broadly applied for unraveling the dynamic and heterogeneous nature of other biologically relevant supramolecular protein complexes.
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