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Thermal proximity coaggregation for system-wide profiling of protein complex dynamics in cells

Tan, Chris Soon Heng ; Go, Ka Diam ; Bisteau, Xavier ; Dai, Lingyun ; Yong, Chern Han ; Prabhu, Nayana ; Ozturk, Mert Burak ; Lim, Yan Ting ; Sreekumar, Lekshmy and Lengqvist, Johan , et al. (2018) In Science (New York, N.Y.) 359(6380). p.1170-1177
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... (More)

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.

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publication status
published
subject
keywords
Cell Line, Cells, Chromatin/metabolism, Hot Temperature, Humans, Multiprotein Complexes/metabolism, Protein Aggregates, Protein Aggregation, Pathological/metabolism, Protein Array Analysis, Protein Biosynthesis, Protein Folding, Proteome
in
Science (New York, N.Y.)
volume
359
issue
6380
pages
8 pages
publisher
American Association for the Advancement of Science
external identifiers
  • scopus:85041895340
  • pmid:29439025
ISSN
1095-9203
DOI
10.1126/science.aan0346
language
English
LU publication?
no
additional info
Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
id
04cf669a-1093-4a98-b3f7-394cd2e18016
date added to LUP
2019-09-17 14:45:08
date last changed
2020-01-22 07:46:28
@article{04cf669a-1093-4a98-b3f7-394cd2e18016,
  abstract     = {<p>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.</p>},
  author       = {Tan, Chris Soon Heng and Go, Ka Diam and Bisteau, Xavier and Dai, Lingyun and Yong, Chern Han and Prabhu, Nayana and Ozturk, Mert Burak and Lim, Yan Ting and Sreekumar, Lekshmy and Lengqvist, Johan and Tergaonkar, Vinay and Kaldis, Philipp and Sobota, Radoslaw M and Nordlund, Pär},
  issn         = {1095-9203},
  language     = {eng},
  month        = {03},
  number       = {6380},
  pages        = {1170--1177},
  publisher    = {American Association for the Advancement of Science},
  series       = {Science (New York, N.Y.)},
  title        = {Thermal proximity coaggregation for system-wide profiling of protein complex dynamics in cells},
  url          = {http://dx.doi.org/10.1126/science.aan0346},
  doi          = {10.1126/science.aan0346},
  volume       = {359},
  year         = {2018},
}