Inside ‐out or outside‐in, a new factor in MAG‐mediated signaling in the nervous system

The integrity and function of the nervous system relies on myelin that is wrapped around axons. The myelin ‐associated glycoprotein MAG has a role in myelin formation and function by organizing signaling and adhesion between myelin and axons. This editorial highlights a study by Myllykoski et al. in which a new factor, DYNLL1, has been identified that binds one of the two splice forms of MAG at the cy tosolic side. The implications of this finding on a role in the adhesion and signalling properties of MAG are described here. AbstractOur 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 organ izes 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 N eurochemistry 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 dimerize...

Source: Journal of Neurochemistry - November 26, 2018 Category: Neurology Authors: Bert J. C. Janssen Tags: Editorial Highlight Source Type: research