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A Global Screen for Assembly State Changes of the Mitotic Proteome by SEC-SWATH-MS.

Authors
  • Heusel, Moritz1
  • Frank, Max2
  • Köhler, Mario3
  • Amon, Sabine2
  • Frommelt, Fabian2
  • Rosenberger, George2
  • Bludau, Isabell2
  • Aulakh, Simran2
  • Linder, Monika I3
  • Liu, Yansheng4
  • Collins, Ben C5
  • Gstaiger, Matthias2
  • Kutay, Ulrike3
  • Aebersold, Ruedi6
  • 1 Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland; Division of Infection Medicine (BMC), Department of Clinical Sciences, Lund University, Lund, Sweden. , (Switzerland)
  • 2 Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland. , (Switzerland)
  • 3 Institute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland. , (Switzerland)
  • 4 Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA.
  • 5 School of Biological Sciences, Queen's University of Belfast, Belfast, UK.
  • 6 Institute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland; Faculty of Science, University of Zurich, Zurich, Switzerland. Electronic address: [email protected] , (Switzerland)
Type
Published Article
Journal
Cell systems
Publication Date
Feb 26, 2020
Volume
10
Issue
2
Identifiers
DOI: 10.1016/j.cels.2020.01.001
PMID: 32027860
Source
Medline
Keywords
Language
English
License
Unknown

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. Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.

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