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Vol. 11, Issue 3, 1093-1101, March 2000
Department of Physiological Chemistry, University of Groningen,
Groningen, the Netherlands
The subapical compartment (SAC) plays an important role in the
polarized transport of proteins and lipids. In hepatoma-derived HepG2
cells, fluorescent analogues of sphingomyelin and
glucosylceramide are sorted in the SAC. Here, evidence is
provided that shows that polarity development is regulated by a
transient activation of endogenous protein kinase A and involves a
transient activation of a specific membrane transport pathway, marked
by the trafficking of the labeled sphingomyelin, from the SAC to the
apical membrane. This protein kinase A-regulated pathway differs from
the apical recycling pathway, which also traverses SAC. After reaching
optimal polarity, the direction of the apically activated pathway
switches to one in the basolateral direction, without affecting the
apical recycling pathway.
Corresponding author. E-mail address:
d.hoekstra{at}med.rug.nl.
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