title: Evolutionarily conserved network properties of intrinsically disordered proteins.
abstract: BACKGROUND
  Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners. Structural flexibility and binding plasticity enable IDPs to interact with a broad range of partners. However, the broader network properties that could provide additional insights into the functional role of IDPs are not known.
  
  
  RESULTS
  Here, we report the first comprehensive survey of network properties of IDP-induced sub-networks in multiple species from yeast to human. Our results show that IDPs exhibit greater-than-expected modularity and are connected to the rest of the protein interaction network (PIN) via proteins that exhibit the highest betweenness centrality and connect to fewer-than-expected IDP communities, suggesting that they form critical communication links from IDP modules to the rest of the PIN. Moreover, we found that IDPs are enriched at the top level of regulatory hierarchy.
  
  
  CONCLUSIONS
  Overall, our analyses reveal coherent and remarkably conserved IDP-centric network properties, namely, modularity in IDP-induced network and a layer of critical nodes connecting IDPs with the rest of the PIN.
authors.affiliation: Indian Institute of Science Education and Research, Pune, India.
authors.forename: Nivedita
authors.initials: N
authors.lastname: Rangarajan
authors.affiliation: Institute for Bioscience & Biotechnology Research, University of Maryland, Rockville, Maryland, United States of America.
authors.forename: Prakash
authors.initials: P
authors.lastname: Kulkarni
authors.affiliation: Center for Bioinformatics and Computational Biology, Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland, United States of America.
authors.forename: Sridhar
authors.initials: S
authors.lastname: Hannenhalli
mesh_terms: D000818:Animals; D016000:Cluster Analysis; D030562:Databases, Protein; D004330:Drosophila / Q000378:metabolism; D029721:Drosophila Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019143:Evolution, Molecular; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D053858:Metabolic Networks and Pathways; D051379:Mice; D009997:Osmotic Pressure; D060066:Protein Interaction Maps; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D029721:Drosophila Proteins; D064267:Intrinsically Disordered Proteins; D029701:Saccharomyces cerevisiae Proteins