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Specificity and Stability in Topology of Protein Networks

Science, 3 May 2002
Vol. 296, Issue 5569, p. 910-913
DOI: 10.1126/science.1065103

Specificity and Stability in Topology of Protein Networks

  1. Sergei Maslov1,*,
  2. Kim Sneppen2
  1. 1 Department of Physics, Brookhaven National Laboratory, Upton, NY 11973, USA.
  2. 2 Department of Physics, Norwegian University of Science and Technology, N-7491 Trondheim, Norway.

Abstract

Molecular networks guide the biochemistry of a living cell on multiple levels: Its metabolic and signaling pathways are shaped by the network of interacting proteins, whose production, in turn, is controlled by the genetic regulatory network. To address topological properties of these two networks, we quantified correlations between connectivities of interacting nodes and compared them to a null model of a network, in which all links were randomly rewired. We found that for both interaction and regulatory networks, links between highly connected proteins are systematically suppressed, whereas those between a highly connected and low-connected pairs of proteins are favored. This effect decreases the likelihood of cross talk between different functional modules of the cell and increases the overall robustness of a network by localizing effects of deleterious perturbations.

  • * To whom correspondence should be addressed. E-mail: maslov{at}bnl.gov

  • Received for publication 6 August 2001.
  • Accepted for publication 25 March 2002.

Citation:

S. Maslov and K. Sneppen, Specificity and Stability in Topology of Protein Networks. Science 296, 910-913 (2002).

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