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- W2034363051 abstract "Myelination within the central nervous system (CNS) involves substantial morphogenesis of oligodendrocytes requiring plastic changes in oligodendrocyte–extracellular matrix (ECM) interactions, that is, adhesion. Our previous studies indicated that a regulator of such adhesive plasticity is oligodendrocyte-released phosphodiesterase-Iα/autotaxin (PD-Iα/ATX). We report here, that PD-Iα/ATX's adhesion antagonism is mediated by a protein fragment different from the one that stimulates tumor cell motility. Furthermore, PD-Iα/ATX's adhesion-antagonizing fragment causes a reorganized distribution of the focal adhesion components vinculin and paxillin and an integrin-dependent reduction in focal adhesion kinase (FAK) phosphorylation at tyrosine residue 925 (pFAK-925). In vivo, a similar reduction in pFAK-925 occurs at the onset of myelination when PD-Iα/ATX expression is significantly upregulated. Most importantly, it can also be induced by the application of exogenous PD-Iα/ATX. Our data, therefore, suggest that PD-Iα/ATX participates in the regulation of myelination via a novel signaling pathway leading to changes in integrin-dependent focal adhesion assembly and consequently oligodendrocyte–ECM interactions." @default.
- W2034363051 created "2016-06-24" @default.
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- W2034363051 date "2004-10-01" @default.
- W2034363051 modified "2023-10-11" @default.
- W2034363051 title "Phosphodiesterase-Iα/autotaxin controls cytoskeletal organization and FAK phosphorylation during myelination" @default.
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- W2034363051 doi "https://doi.org/10.1016/j.mcn.2004.06.002" @default.
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