The Molecular Interplay of Tau and Motor Proteins on Microtubules

Tau suppresses microtubule landing and increases pausing and premature detachment of kinesin-1 and cytoplasmic dynein when motors encounter tau-enriched patches.

• Why it matters: Axonal transport depends on how tau, a microtubule-associated protein, physically regulates motor proteins, but the molecular basis of tau’s inhibition of kinesin-1 and dynein motility was unclear.
• What they did: The authors combined single-molecule imaging, cryo-electron microscopy, and molecular dynamics simulations to test how tau affects kinesin-1 and dynein interactions with tubulin and microtubules.
• The result: Tau blocks kinesin-1 by competing for the same tubulin surface, while it inhibits dynein by preventing dynein’s transition into a high-affinity MT-binding state, providing a structural framework for tau-mediated axonal transport regulation.

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