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Asymmetry between Activators and Deactivators in Functional Protein Networks

Are “turn-on” and “turn-off” functions in protein-protein interaction networks exact opposites of each other? To answer this question, we implement a minimal model for the evolution of functional protein-interaction networks using a sequence-based mutational algorithm, and apply the model to study n...

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Detalles Bibliográficos
Autores principales: Tareen, Ammar, Wingreen, Ned S., Mukhopadhyay, Ranjan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7311538/
https://www.ncbi.nlm.nih.gov/pubmed/32576941
http://dx.doi.org/10.1038/s41598-020-66699-y
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author Tareen, Ammar
Wingreen, Ned S.
Mukhopadhyay, Ranjan
author_facet Tareen, Ammar
Wingreen, Ned S.
Mukhopadhyay, Ranjan
author_sort Tareen, Ammar
collection PubMed
description Are “turn-on” and “turn-off” functions in protein-protein interaction networks exact opposites of each other? To answer this question, we implement a minimal model for the evolution of functional protein-interaction networks using a sequence-based mutational algorithm, and apply the model to study neutral drift in networks that yield oscillatory dynamics. We study the roles of activators and deactivators, two core components of oscillatory protein interaction networks, and find a striking asymmetry in the roles of activating and deactivating proteins, where activating proteins tend to be synergistic and deactivating proteins tend to be competitive.
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spelling pubmed-73115382020-06-25 Asymmetry between Activators and Deactivators in Functional Protein Networks Tareen, Ammar Wingreen, Ned S. Mukhopadhyay, Ranjan Sci Rep Article Are “turn-on” and “turn-off” functions in protein-protein interaction networks exact opposites of each other? To answer this question, we implement a minimal model for the evolution of functional protein-interaction networks using a sequence-based mutational algorithm, and apply the model to study neutral drift in networks that yield oscillatory dynamics. We study the roles of activators and deactivators, two core components of oscillatory protein interaction networks, and find a striking asymmetry in the roles of activating and deactivating proteins, where activating proteins tend to be synergistic and deactivating proteins tend to be competitive. Nature Publishing Group UK 2020-06-23 /pmc/articles/PMC7311538/ /pubmed/32576941 http://dx.doi.org/10.1038/s41598-020-66699-y Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Tareen, Ammar
Wingreen, Ned S.
Mukhopadhyay, Ranjan
Asymmetry between Activators and Deactivators in Functional Protein Networks
title Asymmetry between Activators and Deactivators in Functional Protein Networks
title_full Asymmetry between Activators and Deactivators in Functional Protein Networks
title_fullStr Asymmetry between Activators and Deactivators in Functional Protein Networks
title_full_unstemmed Asymmetry between Activators and Deactivators in Functional Protein Networks
title_short Asymmetry between Activators and Deactivators in Functional Protein Networks
title_sort asymmetry between activators and deactivators in functional protein networks
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7311538/
https://www.ncbi.nlm.nih.gov/pubmed/32576941
http://dx.doi.org/10.1038/s41598-020-66699-y
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