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Vol. 10, Issue 10, 3435-3447, October 1999
Centro de Biología Molecular "Severo Ochoa,"
Universidad Autónoma de Madrid, Consejo Superior de
Investigaciones Científicas, Cantoblanco, 28049 Madrid, Spain
The MAL proteolipid is a nonglycosylated integral membrane protein
found in glycolipid-enriched membrane microdomains. In polarized
epithelial Madin-Darby canine kidney cells, MAL is necessary for normal
apical transport and accurate sorting of the influenza virus
hemagglutinin. MAL is thus part of the integral machinery for
glycolipid-enriched membrane-mediated apical transport. At steady
state, MAL is predominantly located in perinuclear vesicles that
probably arise from the trans-Golgi network (TGN). To
act on membrane traffic and to prevent their accumulation in the target compartment, integral membrane elements of the protein-sorting machinery should be itinerant proteins that cycle between the donor and
target compartments. To establish whether MAL is an itinerant protein,
we engineered the last extracellular loop of MAL by insertion of
sequences containing the FLAG epitope or with sequences containing
residues that became O-glycosylated within the cells or
that displayed biotinylatable groups. The ectopic expression of these
modified MAL proteins allowed us to investigate the surface expression
of MAL and its movement through different compartments after
internalization with the use of a combination of assays, including
surface biotinylation, surface binding of anti-FLAG antibodies,
neuraminidase sensitivity, and drug treatments. Immunofluorescence and
flow cytometric analyses indicated that, in addition to its Golgi
localization, MAL was also expressed on the cell surface, from which it
was rapidly internalized. This retrieval implies transport through the
endosomal pathway and requires endosomal acidification, because it can
be inhibited by drugs such as chloroquine, monensin, and
NH4Cl. Resialylation experiments of surface MAL treated
with neuraminidase indicated that ~30% of the internalized MAL
molecules were delivered to the TGN, probably to start a new cycle of
cargo transport. Together, these observations suggest that, as
predicted for integral membrane members of the late protein transport
machinery, MAL is an itinerant protein cycling between the TGN and the
plasma membrane.
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