The myelin-associated glycoprotein (MAG) is a cell adhesion molecule expres
sed by myelinating glia, existing as two isoforms that differ only by their
cytoplasmic domains. We have studied the in vitro phosphorylation of recom
binant rat MAG cytoplasmic domains by three kinases for which consensus seq
uences exist within this domain, revealing phosphorylation of the L-MAG-spe
cific domain by protein kinase A (PKA). Phosphorylation of the L-MAG cytopl
asmic domain by PKA was decreased in the presence of S100 beta, providing a
functional significance to the interaction between L-MAG and S100 beta, an
d further indicating that L-MAG may play a role in myelinating glial cell s
ignalling processes. (C) 2000 Elsevier Science B.V. All rights reserved.