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J Biol Chem, Vol. 274, Issue 48, 34459-34466, November 26, 1999
From the Department of Biochemistry and Cell Biology, State
University of New York at Stony Brook,
Stony Brook, New York 11794-5215
Recent data suggest that membrane microdomains or
rafts that are rich in sphingolipids and cholesterol are important in
signal transduction and membrane trafficking. Two models of raft
structure have been proposed. One proposes a unique role for
glycosphingolipids (GSL), suggesting that GSL-head-group interactions
are essential in raft formation. The other model suggests that close
packing of the long saturated acyl chains found on both GSL and
sphingomyelin plays a key role and helps these lipids form
liquid-ordered phase domains in the presence of cholesterol. To
distinguish between these models, we compared rafts in the MEB-4
melanoma cell line and its GSL-deficient derivative, GM-95. Rafts were
isolated from cell lysates as detergent-resistant membranes (DRMs). The
two cell lines had very similar DRM protein profiles. The yield of DRM
protein was 2-fold higher in the parental than the mutant line,
possibly reflecting cytoskeletal differences. The same amount of DRM
lipid was isolated from both lines, and the lipid composition was
similar except for up-regulation of sphingomyelin in the mutant that
compensated for the lack of GSL. DRMs from the two lines had similar
fluidity as measured by fluorescence polarization of
diphenylhexatriene. Methyl-
Glycosphingolipids Are Not Essential for Formation of
Detergent-resistant Membrane Rafts in Melanoma Cells
METHYL-
-CYCLODEXTRIN DOES NOT AFFECT CELL SURFACE TRANSPORT
OF A GPI-ANCHORED PROTEIN
-cyclodextrin removed cholesterol from
both cell lines with the same kinetics and to the same extent, and both
a raft-associated glycosyl phosphatidylinositol-anchored protein and
residual cholesterol showed the same distribution between DRMs and the
detergent-soluble fraction after cholesterol removal in both cell
lines. Finally, a glycosyl phosphatidylinositol-anchored protein was
delivered to the cell surface at similar rates in the two lines, even
after cholesterol depletion with methyl--cyclodextrin. We conclude
that GSL are not essential for the formation of rafts and do not play a
major role in determining their properties.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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