Microtubules (MTs) are key components of the eukaryotic cytoskeleton and are involved in major cellular events including cell division, motility and morphogenesis. MTs are organized into stable bundles within axons and dendrites to maintain the polarized shape of neurons and to insure cargo transport. Tau is one of the neuronal MAPs (Microtubule-Associated Proteins) that promote MT assembly and bundling. Although the MT-stabilizing properties of tau have been widely studied, the mechanisms by which this protein spatially organizes MTs remain elusive. By reconstituting in vitro MT bundling, we could identify molecular features involved in MT organization by tau. We used various tau isoforms and truncated fragments either in tau’s N-terminal projection domain or C-terminal MT-binding repeats to decipher the role of each subdomain in MT bundling. We found that the projection…

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