Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes. / Niss, Kristoffer; Gomez-Casado, Cristina; Hjaltelin, Jessica X; Joeris, Thorsten; Agace, William W.; Belling, Kirstine G; Brunak, Søren.

In: Cell Reports, Vol. 31, No. 11, 107763, 2020.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Niss, K, Gomez-Casado, C, Hjaltelin, JX, Joeris, T, Agace, WW, Belling, KG & Brunak, S 2020, 'Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes', Cell Reports, vol. 31, no. 11, 107763. https://doi.org/10.1016/j.celrep.2020.107763

APA

Niss, K., Gomez-Casado, C., Hjaltelin, J. X., Joeris, T., Agace, W. W., Belling, K. G., & Brunak, S. (2020). Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes. Cell Reports, 31(11), [107763]. https://doi.org/10.1016/j.celrep.2020.107763

Vancouver

Niss K, Gomez-Casado C, Hjaltelin JX, Joeris T, Agace WW, Belling KG et al. Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes. Cell Reports. 2020;31(11). 107763. https://doi.org/10.1016/j.celrep.2020.107763

Author

Niss, Kristoffer ; Gomez-Casado, Cristina ; Hjaltelin, Jessica X ; Joeris, Thorsten ; Agace, William W. ; Belling, Kirstine G ; Brunak, Søren. / Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes. In: Cell Reports. 2020 ; Vol. 31, No. 11.

Bibtex

@article{ab53dd2dc5aa459685d202aa681ad23c,
title = "Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes",
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 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.",
author = "Kristoffer Niss and Cristina Gomez-Casado and Hjaltelin, {Jessica X} and Thorsten Joeris and Agace, {William W.} and Belling, {Kirstine G} and S{\o}ren Brunak",
year = "2020",
doi = "10.1016/j.celrep.2020.107763",
language = "English",
volume = "31",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "11",

}

RIS

TY - JOUR

T1 - Complete Topological Mapping of a Cellular Protein Interactome Reveals Bow-Tie Motifs as Ubiquitous Connectors of Protein Complexes

AU - Niss, Kristoffer

AU - Gomez-Casado, Cristina

AU - Hjaltelin, Jessica X

AU - Joeris, Thorsten

AU - Agace, William W.

AU - Belling, Kirstine G

AU - Brunak, Søren

PY - 2020

Y1 - 2020

N2 - 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.

AB - 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.

U2 - 10.1016/j.celrep.2020.107763

DO - 10.1016/j.celrep.2020.107763

M3 - Journal article

C2 - 32553166

VL - 31

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 11

M1 - 107763

ER -

ID: 243475518