Interactions via intrinsically disordered regions: What kind of motifs?

Rita Pancsa, Monika Fuxreiter

Research output: Contribution to journalReview article

50 Citations (Scopus)

Abstract

Proteins containing intrinsically disordered (ID) regions are widespread in eukaryotic organisms and are mostly utilized in regulatory processes. ID regions can mediate binary interactions of proteins or promote organization of large assemblies. Post-translational modifications of ID regions often serve as decision points in signaling pathways. Why Nature distinguished ID proteins in molecular recognition functions? In a simple view, binding of ID regions is accompanied by a large entropic penalty as compared to folded proteins. Even in complexes however, ID regions can preserve their conformational freedom, thereby recruit further partners and perform various functions. What sort of benefits ID regions offer for molecular interactions and which properties are exploited in the corresponding complexes? Here, we review models explaining the recognition mechanisms of ID proteins. Motif-based interactions are central to all proposed scenarios, including prestructured elements, anchoring sites and linear motifs. We aim to extract consensus features of the models, which could be used to predict ID-binding sites for a variety of partners.

Original languageEnglish
Pages (from-to)513-520
Number of pages8
JournalIUBMB life
Volume64
Issue number6
DOIs
Publication statusPublished - Jun 1 2012

Keywords

  • fuzzy complex
  • intrinsically disordered protein
  • linear motif
  • molecular recognition
  • preformed element

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology

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