TY  - JOUR
A1  - Becher, Isabelle
A1  - Andrés-Pons, Amparo
A1  - Romanov, Natalie
A1  - Stein, Frank
A1  - Schramm, Maike
A1  - Baudin, Florence
A1  - Helm, Dominic
A1  - Kurzawa, Nils
A1  - Mateus, André
A1  - Mackmull, Marie-Therese
A1  - Typas, Athanasios
A1  - Müller, Christoph W.
A1  - Bork, Peer
A1  - Beck, Martin
A1  - Savitski, Mikhail M.
T1  - Pervasive Protein Thermal Stability Variation during the Cell Cycle
JF  - Cell
N2  - Quantitative mass spectrometry has established proteome-wide regulation of protein abundance and post-translational modifications in various biological processes. Here, we used quantitative mass spectrometry to systematically analyze the thermal stability and solubility of proteins on a proteome-wide scale during the eukaryotic cell cycle. We demonstrate pervasive variation of these biophysical parameters with most changes occurring in mitosis and G1. Various cellular pathways and components vary in thermal stability, such as cell-cycle factors, polymerases, and chromatin remodelers. We demonstrate that protein thermal stability serves as a proxy for enzyme activity, DNA binding, and complex formation in situ. Strikingly, a large cohort of intrinsically disordered and mitotically phosphorylated proteins is stabilized and solubilized in mitosis, suggesting a fundamental remodeling of the biophysical environment of the mitotic cell. Our data represent a rich resource for cell, structural, and systems biologists interested in proteome regulation during biological transitions.
KW  - thermal proteome profiling
KW  - cell cycle
KW  - proteomics
Y1  - 2018
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-221565
VL  - 173
ER  -