A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS
(2020) In Cell systems 10(2). p.6-155- 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... (More)
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.
(Less)
- author
- organization
- publishing date
- 2020
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- cell cycle, monitoring state of proteome organization, protein complexes, size exclusion chromatography, SWATH-MS
- in
- Cell systems
- volume
- 10
- issue
- 2
- pages
- 6 - 155
- publisher
- Cell Press
- external identifiers
-
- pmid:32027860
- scopus:85079593296
- ISSN
- 2405-4712
- DOI
- 10.1016/j.cels.2020.01.001
- language
- English
- LU publication?
- yes
- id
- 7b65f413-be1c-45e0-8e40-36e3c9356e58
- date added to LUP
- 2020-03-04 09:01:54
- date last changed
- 2024-08-07 14:51:28
@article{7b65f413-be1c-45e0-8e40-36e3c9356e58, abstract = {{<p>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.</p>}}, author = {{Heusel, Moritz and Frank, Max and Köhler, Mario and Amon, Sabine and Frommelt, Fabian and Rosenberger, George and Bludau, Isabell and Aulakh, Simran and Linder, Monika I. and Liu, Yansheng and Collins, Ben C. and Gstaiger, Matthias and Kutay, Ulrike and Aebersold, Ruedi}}, issn = {{2405-4712}}, keywords = {{cell cycle; monitoring state of proteome organization; protein complexes; size exclusion chromatography; SWATH-MS}}, language = {{eng}}, number = {{2}}, pages = {{6--155}}, publisher = {{Cell Press}}, series = {{Cell systems}}, title = {{A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS}}, url = {{http://dx.doi.org/10.1016/j.cels.2020.01.001}}, doi = {{10.1016/j.cels.2020.01.001}}, volume = {{10}}, year = {{2020}}, }