Cargando…

Influence of degree correlations on network structure and stability in protein-protein interaction networks

BACKGROUND: The existence of negative correlations between degrees of interacting proteins is being discussed since such negative degree correlations were found for the large-scale yeast protein-protein interaction (PPI) network of Ito et al. More recent studies observed no such negative correlation...

Descripción completa

Detalles Bibliográficos
Autores principales: Friedel, Caroline C, Zimmer, Ralf
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1995226/
https://www.ncbi.nlm.nih.gov/pubmed/17688687
http://dx.doi.org/10.1186/1471-2105-8-297
_version_ 1782135518012637184
author Friedel, Caroline C
Zimmer, Ralf
author_facet Friedel, Caroline C
Zimmer, Ralf
author_sort Friedel, Caroline C
collection PubMed
description BACKGROUND: The existence of negative correlations between degrees of interacting proteins is being discussed since such negative degree correlations were found for the large-scale yeast protein-protein interaction (PPI) network of Ito et al. More recent studies observed no such negative correlations for high-confidence interaction sets. In this article, we analyzed a range of experimentally derived interaction networks to understand the role and prevalence of degree correlations in PPI networks. We investigated how degree correlations influence the structure of networks and their tolerance against perturbations such as the targeted deletion of hubs. RESULTS: For each PPI network, we simulated uncorrelated, positively and negatively correlated reference networks. Here, a simple model was developed which can create different types of degree correlations in a network without changing the degree distribution. Differences in static properties associated with degree correlations were compared by analyzing the network characteristics of the original PPI and reference networks. Dynamics were compared by simulating the effect of a selective deletion of hubs in all networks. CONCLUSION: Considerable differences between the network types were found for the number of components in the original networks. Negatively correlated networks are fragmented into significantly less components than observed for positively correlated networks. On the other hand, the selective deletion of hubs showed an increased structural tolerance to these deletions for the positively correlated networks. This results in a lower rate of interaction loss in these networks compared to the negatively correlated networks and a decreased disintegration rate. Interestingly, real PPI networks are most similar to the randomly correlated references with respect to all properties analyzed. Thus, although structural properties of networks can be modified considerably by degree correlations, biological PPI networks do not actually seem to make use of this possibility.
format Text
id pubmed-1995226
institution National Center for Biotechnology Information
language English
publishDate 2007
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-19952262007-09-29 Influence of degree correlations on network structure and stability in protein-protein interaction networks Friedel, Caroline C Zimmer, Ralf BMC Bioinformatics Research Article BACKGROUND: The existence of negative correlations between degrees of interacting proteins is being discussed since such negative degree correlations were found for the large-scale yeast protein-protein interaction (PPI) network of Ito et al. More recent studies observed no such negative correlations for high-confidence interaction sets. In this article, we analyzed a range of experimentally derived interaction networks to understand the role and prevalence of degree correlations in PPI networks. We investigated how degree correlations influence the structure of networks and their tolerance against perturbations such as the targeted deletion of hubs. RESULTS: For each PPI network, we simulated uncorrelated, positively and negatively correlated reference networks. Here, a simple model was developed which can create different types of degree correlations in a network without changing the degree distribution. Differences in static properties associated with degree correlations were compared by analyzing the network characteristics of the original PPI and reference networks. Dynamics were compared by simulating the effect of a selective deletion of hubs in all networks. CONCLUSION: Considerable differences between the network types were found for the number of components in the original networks. Negatively correlated networks are fragmented into significantly less components than observed for positively correlated networks. On the other hand, the selective deletion of hubs showed an increased structural tolerance to these deletions for the positively correlated networks. This results in a lower rate of interaction loss in these networks compared to the negatively correlated networks and a decreased disintegration rate. Interestingly, real PPI networks are most similar to the randomly correlated references with respect to all properties analyzed. Thus, although structural properties of networks can be modified considerably by degree correlations, biological PPI networks do not actually seem to make use of this possibility. BioMed Central 2007-08-09 /pmc/articles/PMC1995226/ /pubmed/17688687 http://dx.doi.org/10.1186/1471-2105-8-297 Text en Copyright © 2007 Friedel and Zimmer; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Friedel, Caroline C
Zimmer, Ralf
Influence of degree correlations on network structure and stability in protein-protein interaction networks
title Influence of degree correlations on network structure and stability in protein-protein interaction networks
title_full Influence of degree correlations on network structure and stability in protein-protein interaction networks
title_fullStr Influence of degree correlations on network structure and stability in protein-protein interaction networks
title_full_unstemmed Influence of degree correlations on network structure and stability in protein-protein interaction networks
title_short Influence of degree correlations on network structure and stability in protein-protein interaction networks
title_sort influence of degree correlations on network structure and stability in protein-protein interaction networks
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1995226/
https://www.ncbi.nlm.nih.gov/pubmed/17688687
http://dx.doi.org/10.1186/1471-2105-8-297
work_keys_str_mv AT friedelcarolinec influenceofdegreecorrelationsonnetworkstructureandstabilityinproteinproteininteractionnetworks
AT zimmerralf influenceofdegreecorrelationsonnetworkstructureandstabilityinproteinproteininteractionnetworks