Dynamic interactions of proteins in complex networks: a more structured view

FEBS J. 2009 Oct;276(19):5390-405. doi: 10.1111/j.1742-4658.2009.07251.x. Epub 2009 Aug 27.


Virtually every process in a cell is carried out by macromolecular complexes whose actions need to be perfectly orchestrated. The synchronization and regulation of these biological functions is indeed critical and is usually carried out by complex networks of transient protein interactions. Here, we review some of the many strategies that proteins in regulatory networks use to achieve the dynamic plasticity necessary to rapidly respond to diverse cellular needs. More specifically, we present recent work on the molecular bases of transient peptide-mediated interactions and the role that post-translational modifications and disordered regions might play. Finally, in light of some recent findings, we speculate on the possibility of a new regulatory code for intrinsically disordered proteins and the potential biophysical and functional advantages that disorder might provide.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Humans
  • MAP Kinase Signaling System
  • Metabolic Networks and Pathways
  • Models, Molecular
  • Phosphorylation
  • Protein Binding
  • Protein Folding
  • Protein Interaction Domains and Motifs / physiology*
  • Protein Interaction Mapping
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Signal Transduction