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Vol. 10, Issue 10, 3449-3461, October 1999
Department of Physiological Chemistry, Faculty of Medical Sciences,
University of Groningen, 9713 AV Groningen, The Netherlands
In polarized HepG2 cells, the sphingolipids glucosylceramide and
sphingomyelin (SM), transported along the reverse transcytotic pathway,
are sorted in subapical compartments (SACs), and subsequently targeted
to either apical or basolateral plasma membrane domains, respectively. In the present study, evidence is provided that demonstrates that these sphingolipids constitute separate membrane domains at the luminal side of the SAC membrane. Furthermore, as
revealed by the use of various modulators of membrane trafficking, such
as calmodulin antagonists and dibutyryl-cAMP, it is shown that the fate
of these separate sphingolipid domains is regulated by different
signals, including those that govern cell polarity development. Thus
under conditions that stimulate apical plasma membrane biogenesis, SM
is rerouted from a SAC-to-basolateral to a SAC-to-apical pathway. The
latter pathway represents the final leg in the transcytotic pathway,
followed by the transcytotic pIgR-dIgA protein complex. Interestingly,
this pathway is clearly different from the apical recycling pathway
followed by glucosylceramide, further indicating that randomization of
these pathways, which are both bound for the apical membrane, does not
occur. The consequence of the potential coexistence of separate
sphingolipid domains within the same compartment in terms of "raft"
formation and apical targeting is discussed.
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