S100β inhibits the phosphorylation of the L-MAG cytoplasmic domain by PKA

The myelin-associated glycoprotein (MAG) is a cell adhesion molecule expressed by myelinating glia, existing as two isoforms that differ only by their cytoplasmic domains. We have studied the in vitro phosphorylation of recombinant rat MAG cytoplasmic domains by three kinases for which consensus seq...

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Bibliographic Details
Published in:Brain research. Molecular brain research. 2000-03, Vol.76 (2), p.407-410
Main Authors: Kursula, Petri, Lehto, Veli-Pekka, Heape, Anthony M
Format: Article
Language:English
Subjects:
Biological and medical sciences
Cell physiology
Fundamental and applied biological sciences. Psychology
Miscellaneous
Molecular and cellular biology
Myelin
Myelin-associated glycoprotein
Phosphorylation
Protein kinase A
S100 protein
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Summary:The myelin-associated glycoprotein (MAG) is a cell adhesion molecule expressed by myelinating glia, existing as two isoforms that differ only by their cytoplasmic domains. We have studied the in vitro phosphorylation of recombinant rat MAG cytoplasmic domains by three kinases for which consensus sequences exist within this domain, revealing phosphorylation of the L-MAG-specific domain by protein kinase A (PKA). Phosphorylation of the L-MAG cytoplasmic domain by PKA was decreased in the presence of S100β, providing a functional significance to the interaction between L-MAG and S100β, and further indicating that L-MAG may play a role in myelinating glial cell signalling processes.
ISSN:0169-328X
1872-6941
DOI:10.1016/S0169-328X(00)00018-8