Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes
(2020) In Cell Reports 31(11).- Abstract
The network topology of a protein interactome is shaped by the function of each protein, making it a resource of functional knowledge in tissues and in single cells. Today, this resource is underused, as complete network topology characterization has proved difficult for large protein interactomes. We apply a matrix visualization and decoding approach to a physical protein interactome of a dendritic cell, thereby characterizing its topology with no prior assumptions of structure. We discover 294 proteins, each forming topological motifs called “bow-ties” that tie together the majority of observed protein complexes. The central proteins of these bow-ties have unique network properties, display multifunctional capabilities, are enriched... (More)
The network topology of a protein interactome is shaped by the function of each protein, making it a resource of functional knowledge in tissues and in single cells. Today, this resource is underused, as complete network topology characterization has proved difficult for large protein interactomes. We apply a matrix visualization and decoding approach to a physical protein interactome of a dendritic cell, thereby characterizing its topology with no prior assumptions of structure. We discover 294 proteins, each forming topological motifs called “bow-ties” that tie together the majority of observed protein complexes. The central proteins of these bow-ties have unique network properties, display multifunctional capabilities, are enriched for essential proteins, and are widely expressed in other cells and tissues. Collectively, the bow-tie motifs are a pervasive and previously unnoted topological trend in cellular interactomes. As such, these results provide fundamental knowledge on how intracellular protein connectivity is organized and operates. Niss et al. show that topological motifs called bow-ties create a scaffold within the cellular protein interactome that connects a majority of protein complexes. The central proteins of these motifs are found to be associated with multifunctionality and cellular essentiality, display unique network properties, and are expressed widely across cells and tissues.
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- author
- Niss, Kristoffer ; Gomez-Casado, Cristina LU ; Hjaltelin, Jessica X. ; Joeris, Thorsten LU ; Agace, William W. LU ; Belling, Kirstine G. and Brunak, Søren
- organization
- publishing date
- 2020-06-16
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- biological networks, bow-tie, essential, functional organization, knot protein, multifunctional, network motifs, network topology, protein complex, topological overlap
- in
- Cell Reports
- volume
- 31
- issue
- 11
- article number
- 107763
- publisher
- Cell Press
- external identifiers
-
- scopus:85086362850
- pmid:32553166
- ISSN
- 2211-1247
- DOI
- 10.1016/j.celrep.2020.107763
- language
- English
- LU publication?
- yes
- id
- a882df68-b5c7-4a16-b66c-59cf28deffbc
- date added to LUP
- 2020-06-22 20:25:59
- date last changed
- 2024-06-12 16:03:27
@article{a882df68-b5c7-4a16-b66c-59cf28deffbc,
abstract = {{<p>The network topology of a protein interactome is shaped by the function of each protein, making it a resource of functional knowledge in tissues and in single cells. Today, this resource is underused, as complete network topology characterization has proved difficult for large protein interactomes. We apply a matrix visualization and decoding approach to a physical protein interactome of a dendritic cell, thereby characterizing its topology with no prior assumptions of structure. We discover 294 proteins, each forming topological motifs called “bow-ties” that tie together the majority of observed protein complexes. The central proteins of these bow-ties have unique network properties, display multifunctional capabilities, are enriched for essential proteins, and are widely expressed in other cells and tissues. Collectively, the bow-tie motifs are a pervasive and previously unnoted topological trend in cellular interactomes. As such, these results provide fundamental knowledge on how intracellular protein connectivity is organized and operates. Niss et al. show that topological motifs called bow-ties create a scaffold within the cellular protein interactome that connects a majority of protein complexes. The central proteins of these motifs are found to be associated with multifunctionality and cellular essentiality, display unique network properties, and are expressed widely across cells and tissues.</p>}},
author = {{Niss, Kristoffer and Gomez-Casado, Cristina and Hjaltelin, Jessica X. and Joeris, Thorsten and Agace, William W. and Belling, Kirstine G. and Brunak, Søren}},
issn = {{2211-1247}},
keywords = {{biological networks; bow-tie; essential; functional organization; knot protein; multifunctional; network motifs; network topology; protein complex; topological overlap}},
language = {{eng}},
month = {{06}},
number = {{11}},
publisher = {{Cell Press}},
series = {{Cell Reports}},
title = {{Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes}},
url = {{http://dx.doi.org/10.1016/j.celrep.2020.107763}},
doi = {{10.1016/j.celrep.2020.107763}},
volume = {{31}},
year = {{2020}},
}