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J Biol Chem, Vol. 274, Issue 41, 29042-29049, October 8, 1999
From the Department of Neurobiology, University of Heidelberg, Im
Neuenheimer Feld 364, 69120 Heidelberg, Germany
In many cell types, glycosylphosphatidylinositol
(GPI)-anchored proteins are sequestered in detergent-resistant membrane
rafts. These are plasma membrane microdomains enriched in
glycosphingolipids and cholesterol and are suggested to be platforms
for cell signaling. Concomitant with the synthesis of myelin
glycosphingolipids, maturing oligodendrocytes progressively associate
GPI-anchored proteins, including the adhesion molecules NCAM 120 and
F3, in rafts. Here we show that these microdomains include Fyn and Lyn
kinases. Both kinases are maximally active in myelin prepared from
young animals, correlating with early stages of myelination. In the
rafts, Fyn kinase is tightly associated with NCAM 120 and F3. In
contrast, in oligodendrocyte progenitor cells lacking rafts or in
raft-free membrane domains of more mature cells, F3 does not associate
with Fyn. The addition of anti-F3 antibodies to oligodendrocytes
results in stimulation of Fyn kinase specifically in rafts.
Compartmentation of oligodendrocyte GPI-anchored proteins in rafts is
thus a prerequisite for association with Fyn, permitting kinase
activation. Interaction of oligodendrocyte F3 with axonal ligands such
as L1 and ensuing kinase activation may play a crucial role in
initiating myelination.
Compartmentation of Fyn Kinase with
Glycosylphosphatidylinositol-anchored Molecules in Oligodendrocytes
Facilitates Kinase Activation during Myelination
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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