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|Title:||Thermal proximity coaggregation for system-wide profiling of protein complex dynamics in cells||Authors:||Tan, Chris Soon Heng
Go, Ka Diam
Yong, Chern Han
Ozturk, Mert Burak
Lim, Yan Ting
Sobota, Radoslaw M.
Cellular Thermal Shift Assay
Protein Interaction Network
|Issue Date:||2018||Source:||Tan, C. S. H., Go, K. D., Bisteau, X., Dai, L., Yong, C. H., Prabhu, N., . . . Nordlund, P. (2018). Thermal proximity coaggregation for system-wide profiling of protein complex dynamics in cells. Science, 359(6380), 1170-1177. doi:10.1126/science.aan0346||Series/Report no.:||Science||Abstract:||Proteins differentially interact with each other across cellular states and conditions, but an efficient proteome-wide strategy to monitor them is lacking. We report the application of thermal proximity coaggregation (TPCA) for high-throughput intracellular monitoring of protein complex dynamics. Significant TPCA signatures observed among well-validated protein-protein interactions correlate positively with interaction stoichiometry and are statistically observable in more than 350 annotated human protein complexes. Using TPCA, we identified many complexes without detectable differential protein expression, including chromatin-associated complexes, modulated in S phase of the cell cycle. Comparison of six cell lines by TPCA revealed cell-specific interactions even in fundamental cellular processes. TPCA constitutes an approach for system-wide studies of protein complexes in nonengineered cells and tissues and might be used to identify protein complexes that are modulated in diseases.||URI:||https://hdl.handle.net/10356/90293
|ISSN:||0036-8075||DOI:||10.1126/science.aan0346||Rights:||© 2017 The Authors. All rights reserved. This paper was published by American Association for the Advancement of Science in Science and is made available with permission of The Authors.||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Journal Articles|
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