Thermal proximity coaggregation for system-wide profiling of protein complex dynamics in cells
(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.
(Less)
- author
- publishing date
- 2018-03-09
- type
- Contribution to journal
- 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 (AAAS)
- external identifiers
-
- pmid:29439025
- scopus:85041895340
- 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
- 2024-09-04 09:19:46
@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}}, 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}}, language = {{eng}}, month = {{03}}, number = {{6380}}, pages = {{1170--1177}}, publisher = {{American Association for the Advancement of Science (AAAS)}}, 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}}, }