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Calcium‐Dependent Interaction Between the Large Myelin‐Associated Glycoprotein and S100β
Author(s) -
Kursula Petri,
Tikkanen Gitte,
Lehto VeliPekka,
Nishikimi Morimitsu,
Heape Anthony
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.731724.x
Subject(s) - myelin , glycoprotein , myelin associated glycoprotein , microbiology and biotechnology , gene isoform , oligodendrocyte , biology , cytoplasm , biochemistry , transmembrane protein , calcium , chemistry , receptor , central nervous system , neuroscience , organic chemistry , gene
: The myelin‐associated glycoprotein is a transmembrane cell adhesion molecule expressed by myelinating glial cells of the nervous system. So far, only protein kinases have been reported to interact with the cytoplasmic domains of the two isoforms of the myelinassociated glycoprotein. We report here the identification of the first nonkinase intracellular ligand for the large isoform of the myelin‐associated glycoprotein as the S100β protein. The interaction is dependent on the presence of calcium. We have also localized the S100β‐binding site in the cytoplasmic domain specific to the large myelin‐associated glycoprotein isoform to a putative basic amphipathic α‐helix. A synthetic peptide corresponding to this region bound to S100β in a calcium‐dependent manner with a stoichiometric ratio of 1:1 ( K D ≈ 7 μ M ). We suggest that the observed interaction may play a role in the regulation of the myelinating glial cell cytoskeleton and the divalent cation‐dependent signal transduction events during myelin formation and maintenance.