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J. Biol. Chem., Vol. 278, Issue 1, 164-173, January 3, 2003
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From the Department of Membrane Cell Biology, Faculty of Medical
Sciences, University of Groningen, A. Deusinglaan 1, 9713 AV Groningen, The Netherlands
In HepG2 cells, the subapical compartment (SAC)
is involved in the biogenesis of membrane polarity. By contrast, direct
apical transport originating from the trans-Golgi network (TGN), which may contribute to polarity establishment, has been poorly defined in
these cells. Thus, although newly synthesized sphingolipids can be
directly transported from the TGN to the apical membrane, numerous
apical resident proteins are traveling via the transcytotic route.
Here, we developed an in vitro transport assay and compared the molecular sorting of 6-[N-(7-nitrobenz-2-oxa-1,3
diazol-4-yl)amino] hexanoyl-sphingomyelin (C6NBD-SM) and
C6NBD-glucosylceramide (C6NBD-GlcCer) in TGN
and SAC. SM is released from both TGN and SAC in the lumenal leaflet of
transport vesicles. This holds also for GlcCer released from the SAC
but not for a substantial fraction that departed from the Golgi.
Distinct transport vesicles, enriched in either SM or GlcCer are
released from SAC, consistent with their rigid sorting in this
compartment. Different vesicle populations could not be recovered from
TGN, although in situ experiments reveal that GlcCer is
preferentially transported to the apical membrane, reflecting different
transport mechanisms. The results indicate that in HepG2 cells
sphingolipids are mainly sorted in the SAC membrane and that the
release of SM from SAC and TGN is differentially regulated.
Trans-Golgi Network and Subapical Compartment of HepG2 Cells
Display Different Properties in Sorting and Exiting of
Sphingolipids*
and
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by Grant BMBF-LPD 9801-21 from the Deutsche
Akademie der Naturforscher Leopoldina.
§
To whom correspondence should be addressed. Tel.:
31-50-363-2741; Fax: 31-50-363-2728; E-mail:
d.hoekstra@med.rug.nl.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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