Kinetically distinct phases of tau on microtubules regulate kinesin motors and severing enzymes

Research output: Contribution to journalLetterContributedpeer-review


  • Valerie Siahaan - , Czech Academy of Sciences (Author)
  • Jochen Krattenmacher - , Czech Academy of Sciences (Author)
  • Anthony A. Hyman - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Stefan Diez - , Chair of BioNano-Tools, Clusters of Excellence PoL: Physics of Life, Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Amayra Hernández-Vega - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Zdenek Lansky - , Czech Academy of Sciences (Author)
  • Marcus Braun - , Czech Academy of Sciences (Author)


Tau is an intrinsically disordered protein, which diffuses on microtubules1. In neurodegenerative diseases, collectively termed tauopathies, malfunction of tau and its detachment from axonal microtubules are correlated with axonal degeneration2. Tau can protect microtubules from microtubule-degrading enzymes such as katanin3. However, how tau carries out this regulatory function is still unclear. Here, using in vitro reconstitution, we show that tau molecules on microtubules cooperatively form cohesive islands that are kinetically distinct from tau molecules that individually diffuse on microtubules. Dependent on the tau concentration in solution, the islands reversibly grow or shrink by addition or release of tau molecules at their boundaries. Shielding microtubules from kinesin-1 motors and katanin, the islands exhibit regulatory qualities distinct from a comparably dense layer of diffusible tau. Superprocessive kinesin-8 motors penetrate the islands and cause their disassembly. Our results reveal a microtubule-dependent phase of tau that constitutes an adaptable protective layer on the microtubule surface. We anticipate that other intrinsically disordered axonal proteins display a similar cooperative behaviour and potentially compete with tau in regulating access to the microtubule surface.


Original languageEnglish
Pages (from-to)1086-1092
Number of pages7
JournalNature cell biology
Issue number9
Publication statusPublished - 1 Sept 2019

External IDs

PubMed 31481789
ORCID /0000-0002-0750-8515/work/142235554


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ASJC Scopus subject areas