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Vol. 14, Issue 2, 611-624, February 2003
*Department of Membrane Cell Biology, University of
Groningen, 9713 AV Groningen, The Netherlands; and
In polarized hepatic cells, pathways and molecular principles
mediating the flow of resident apical bile canalicular proteins have not yet been resolved. Herein, we have investigated apical trafficking of a glycosylphosphatidylinositol-linked and two
single transmembrane domain proteins on the one hand, and two polytopic proteins on the other in polarized HepG2 cells. We demonstrate that the
former arrive at the bile canalicular membrane via the indirect
transcytotic pathway, whereas the polytopic proteins reach the apical
membrane directly, after Golgi exit. Most importantly, cholesterol-based lipid microdomains ("rafts") are operating in either pathway, and protein sorting into such domains occurs in the
biosynthetic pathway, largely in the Golgi. Interestingly, rafts
involved in the direct pathway are Lubrol WX insoluble but Triton X-100
soluble, whereas rafts in the indirect pathway are both Lubrol WX and
Triton X-100 insoluble. Moreover, whereas cholesterol depletion alters
raft-detergent insolubility in the indirect pathway without affecting
apical sorting, protein missorting occurs in the direct pathway without
affecting raft insolubility. The data implicate cholesterol as a
traffic direction-determining parameter in the direct apical pathway.
Furthermore, raft-cargo likely distinguishing single vs. multispanning
membrane anchors, rather than rafts per se (co)determine the sorting pathway.
U538 Institut National de la Santé et de
la Recherche Médicale, 75571 Paris, France
Corresponding author. E-mail address:
d.hoekstra{at}med.rug.nl
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