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Rapid, optimized interactomic screening

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  • Zhanna Hakhverdyan, United States
  • Michal Domanski
  • ,
  • Loren E Hough, United States
  • Asha A Oroskar, United States
  • Anil R Oroskar, United States
  • Sarah Keegan, United States
  • David J Dilworth, United States
  • Kelly R Molloy, United States
  • Vadim Sherman, United States
  • John D Aitchison, United States
  • David Fenyö, United States
  • Brian T Chait, United States
  • Torben Heick Jensen
  • Michael P Rout, United States
  • John LaCava, United States

We must reliably map the interactomes of cellular macromolecular complexes in order to fully explore and understand biological systems. However, there are no methods to accurately predict how to capture a given macromolecular complex with its physiological binding partners. Here, we present a screening method that comprehensively explores the parameters affecting the stability of interactions in affinity-captured complexes, enabling the discovery of physiological binding partners in unparalleled detail. We have implemented this screen on several macromolecular complexes from a variety of organisms, revealing novel profiles for even well-studied proteins. Our approach is robust, economical and automatable, providing inroads to the rigorous, systematic dissection of cellular interactomes.

Original languageEnglish
JournalNature Methods
Volume12
Issue6
Pages (from-to)553-560
Number of pages8
ISSN1548-7091
DOIs
Publication statusPublished - Jun 2015

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