Stochastic machines as a colocalization mechanism for scaffold protein function

Bin Xue, Pedro R. Romero, Maria Noutsou, Madelon M. Maurice, Stefan G.D. Rüdiger, Albert M. William, Marcin J. Mizianty, Lukasz Kurgan, Vladimir N. Uversky, A. Keith Dunker

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


The axis inhibition (Axin) scaffold protein colocalizes β-catenin, casein kinase Iα, and glycogen synthetase kinase 3β by their binding to Axin's long intrinsically disordered region, thereby yielding structured domains with flexible linkers. This complex leads to the phosphorylation of β-catenin, marking it for destruction. Fusing proteins with flexible linkers vastly accelerates chemical interactions between them by their colocalization. Here we propose that the complex works by random movements of a "stochastic machine," not by coordinated conformational changes. This non-covalent, modular assembly process allows the various molecular machine components to be used in multiple processes.

Original languageEnglish (US)
Pages (from-to)1587-1591
Number of pages5
JournalFEBS Letters
Issue number11
StatePublished - Jun 5 2013


  • Molecular machines
  • Protein complexes
  • Scaffold proteins
  • Signaling

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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