Unraveling the etiology of myelin disorders: the P2 case in Charcot–Marie–Tooth disease

PUSTERLA, JULIO; MONTICH, GUILLERMO G.; OLIVEIRA, RAFAEL G.

FEBS JOURNAL

WILEY-BLACKWELL PUBLISHING, INC

Año: 2021

1742-464X

here are several examples of single mutations that lead to a well-defined disease through a well-known mechanism. In other cases, a collection of mutations of the same protein produces a pathology with different degrees of severity. The accompanying work by Uusitalo et al. studies several mutants of the fatty acid binding protein P2 of the peripheral nervous system myelin. They conserve the native tertiary structure but a remarkable difference in the capacity to interact with lipids. This could be a clue to unravel the complex way in which these mutations affect myelin structure and function in a variant of Charcot-Marie-Tooth disease. Comment on: https://doi.org/10.1111/febs.16079.