S100 beta inhibits the phosphorylation of the L-MAG cytoplasmic domain by PKA

Citation
P. Kursula et al., S100 beta inhibits the phosphorylation of the L-MAG cytoplasmic domain by PKA, MOL BRAIN R, 76(2), 2000, pp. 407-410
Citations number
28
Categorie Soggetti
Neurosciences & Behavoir
Journal title
MOLECULAR BRAIN RESEARCH
ISSN journal
0169328X → ACNP
Volume
76
Issue
2
Year of publication
2000
Pages
407 - 410
Database
ISI
SICI code
0169-328X(20000329)76:2<407:SBITPO>2.0.ZU;2-P
Abstract
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.