A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS.
Cell Syst
; 10(2): 133-155.e6, 2020 02 26.
Article
em En
| MEDLINE
| ID: mdl-32027860
ABSTRACT
Living systems integrate biochemical reactions that determine the functional state of each cell. Reactions are primarily mediated by proteins. In proteomic studies, these have been treated as independent entities, disregarding their higher-level organization into complexes that affects their activity and/or function and is thus of great interest for biological research. Here, we describe the implementation of an integrated technique to quantify cell-state-specific changes in the physical arrangement of protein complexes concurrently for thousands of proteins and hundreds of complexes. Applying this technique to a comparison of human cells in interphase and mitosis, we provide a systematic overview of mitotic proteome reorganization. The results recall key hallmarks of mitotic complex remodeling and suggest a model of nuclear pore complex disassembly, which we validate by orthogonal methods. To support the interpretation of quantitative SEC-SWATH-MS datasets, we extend the software CCprofiler and provide an interactive exploration tool, SECexplorer-cc.
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Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteômica
/
Espectrometria de Massas em Tandem
/
Mitose
Limite:
Humans
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article