Microtubules composed of  tubulin heterodimer units undergo constant growth and shrinkage. This property is defined as dynamic instability, which is an integral part of the cellular activity. In neurons, the dynamic microtubules are present together with stable microtubules. Several microtubule-associated proteins (MAP) have been characterized for regulating dynamic microtubules, however the molecular mechanisms used to stabilise microtubules are largely unknown. Our team study the neuronal microtubule stabiliser MAP6 for several years and showed recently that MAP6 binds inside and outside the microtubule cylinder. Deciphering at the molecular level how MAP6 binds to microtubules (outside and inside) will help to understand how this microtubule associated protein increases the stability of microtubules in neurons.