Microtubules Gate Tau Condensation to Spatially Regulate Microtubule Functions
Preprint posted on 22 September 2018 https://www.biorxiv.org/content/early/2018/09/22/423376
Article now published in Nature Cell Biology at http://dx.doi.org/10.1038/s41556-019-0375-5
Kinetically distinct phases of tau on microtubules regulate kinesin motors and severing enzymes
Preprint posted on 22 September 2018 https://www.biorxiv.org/content/early/2018/09/22/424374
Article now published in Nature Cell Biology at http://dx.doi.org/10.1038/s41556-019-0374-6
Islands on the highways! The microtubule-associated protein tau forms reversible islands on microtubules in vitro and modulates the behavior of motor proteins and severing enzymes.
Selected by Satish BodakuntlaCategories: biochemistry, biophysics, cell biology
Context: Ever since the discovery of microtubule-associated proteins (MAPs) in the 1970s, tau has received particular interest as it is involved in a number of neurodegenerative diseases and undergoes diverse molecular behaviours (tau aggregation and tau phase separation droplets). While tau was shown to regulate microtubule interactions of several MAPs including motor proteins and severing enzymes, the underlying mechanisms remained largely elusive. In these preprints, the authors show that tau forms reversible condensates on the microtubules in vitro and reveal how these condensates regulate the microtubule interaction of severing enzymes and molecular motors.
Key findings: The authors used in vitro reconstitution assays and observed that tau binds microtubules in a non-homogenous manner, i.e. some regions of microtubules are densely decorated with tau molecules, termed ‘tau condensates’ or ‘tau islands’. These condensates can grow and shrink along the microtubule, merge with the nearby condensates and are reversible upon removal of tau from the solution. Consistent with earlier in vivo data showing that tau prevents microtubule severing, the authors observed that tau islands efficiently protect the microtubules from katanin and spastin mediated-severing. Interestingly, these tau islands selectively form barriers on microtubules to regulate the movement of molecular motors. While highly processive molecular motors, like dynein and kinesin-8 could efficiently pass through the condensates, kinesin-1 motors could not penetrate the tau islands. Overall, the authors present a novel idea that tau condensation is in fact a physiological form of tau self-association and thereby explain the physiological importance of tau oligomerization in mediating its functions.
Why this preprint is interesting: Microtubules, formed by well-conserved tubulin heterodimers, must functionally specialize to perform a plethora of diverse functions, which many times is attained by interacting with several MAPs. Strikingly, in these preprints, the authors go one step ahead and show how an individual MAP – tau – by forming two distinct phases spatially confers different properties to microtubules. Further, the observations made by the authors raise very intriguing questions for the microtubule community.
Questions the work raises: The preprints complement each other well to strengthen their hypothesis and to address possible questions in the scope of their study. That said, their results raise intriguing questions for the follow-up studies.
- Why do tau condensates form islands specifically in some regions of microtubules?
- Why does tau form condensates only on taxol-stabilised microtubules and not on GMP-CPP microtubules?
- Can other microtubule-associated proteins also form condensates or islands?
Posted on: 12 December 2018 , updated on: 19 December 2018
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