Petri Kursula lab
Molecules of myelination

Unraveling the mysteries of myelin maturation

The molecular processes of myelin maturation are to a large extent still unknown. A coordinated interplay between regulatory and functional molecules must take place for correct timing of myelin membrane apposition and compaction, such that cytoplasmic channels are also formed in a correct way.


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In collaboration with Prof. Mikael Simons (Göttingen/München), we showed that antagonistic functions of two classical myelin proteins, MBP and CNPase, are important for the formation of myelin cytoplasmic channels. This regulation also involves the actin cytoskeleton of the myelinating glial cell. We showed that CNPase directly binds to actin microfilaments, and using structural biology data, we could map the interaction sites. An important implication of the results is that the enzymatic activity of CNPase seems to be redundant for this function, and CNPase behaves like a structural protein. 

Snaidero N., Velte C., Myllykoski M., Raasakka A., Ignatev A., Werner H.B., Erwig M.S., Möbius W., Kursula P., Nave K.A. & Simons M. (2017) Antagonistic functions of MBP and CNP establish cytosolic channels in CNS myelin. Cell Rep. 18:314-323.