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Vol. 11, Issue 6, 2033-2045, June 2000
Centro de Biología Molecular "Severo Ochoa,"
Universidad Autónoma de Madrid, and Consejo Superior de
Investigaciones Científicas, 28049 Madrid, Spain
The MAL proteolipid has been recently demonstrated as being
necessary for correct apical sorting of the transmembrane influenza virus hemagglutinin (HA) in Madin-Darby canine kidney (MDCK) cells. The fact that, in contrast to MDCK cells, Fischer rat thyroid (FRT)
cells target the majority of glycosylphosphatidylinositol (GPI)-anchored proteins to the basolateral membrane provides us with
the opportunity to determine the role of MAL in apical transport of
membrane proteins under conditions in which the majority of GPI-anchored proteins are (MDCK cells) or are not (FRT cells) targeted
to the apical surface. Using an antisense oligonucleotide-based strategy to deplete endogenous MAL, we have observed that correct transport of apical transmembrane proteins associated (HA) or not
(exogenous neurotrophin receptor and endogenous dipeptidyl peptidase
IV) with lipid rafts, as well as that of the bulk of endogenous apical
membrane, takes place in FRT cells by a pathway that requires normal
MAL levels. Even transport of placental alkaline phosphatase, a
GPI-anchored protein that is targeted apically in FRT cells, was
dependent on normal MAL levels. Similarly, in addition to the reported
effect of MAL on HA transport, depletion of MAL in MDCK cells caused a
dramatic reduction in the apical delivery of the GPI-anchored gD1-DAF
protein, neurotrophin receptor, and the bulk of membrane proteins.
These results suggest that MAL is necessary for the overall apical
transport of membrane proteins in polarized MDCK and FRT cells.
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