Inside-out or outside-in, a new factor in MAG-mediated signaling in the nervous system: An Editorial for 'High-affinity heterotetramer formation between the large myelin-associated glycoprotein and the dynein light chain DYNLL1' on doi:10.1111/jnc.14598.

Our nervous system depends on protein-mediated cellular communication and connections for its formation and function. The transmembrane receptor Myelin-Associated Glycoprotein (MAG) plays an important role in the wrapping process of myelin around axons and in life-long maintenance of this important bicellular structure. MAG organizes the adhesion and the signalling between the axon and the myelin. But how does MAG do this? Better understanding of this process is required to treat MAG-function associated neurological disorders. This editorial highlights a study by Myllykoski et al. in the current issue of the Journal of Neurochemistry that describes the identification and characterization of a novel intracellular binding partner of MAG. Using cellular, biophysical and structural techniques, the authors show that the dynein light chain, DYNLL1 recognizes and interacts with only one of two splice forms of MAG, L-MAG. DYNLL1 dimerizes L-MAG at the cytosolic side and this has implications for the signalling and adhesive functions of MAG in our nervous system.