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Department of Molecular Microbiology and Immunology, Oregon Health Sciences University, Portland, Oregon 97201
The major glucose transporter of the parasitic protozoan Leishmania enriettii exists in two isoforms, one of which (iso-1) localizes to the flagellar
membrane, while the other (iso-2) localizes to the
plasma membrane of the cell body, the pellicular membrane. These two isoforms differ only in their cytosolic
NH2-terminal domains. Using immunoblots and immunofluorescence microscopy of detergent-extracted cytoskeletons, we have demonstrated that iso-2 associates
with the microtubular cytoskeleton that underlies the cell body membrane, whereas the flagellar membrane
isoform iso-1 does not associate with the cytoskeleton.
Deletion mutants that remove the first 25 or more
amino acids from iso-1 are retargeted from the flagellum to the pellicular membrane, suggesting that these
deletions remove a signal required for flagellar targeting. Unlike the full-length iso-1 protein, these deletion
mutants associate with the cytoskeleton. Our results
suggest that cytoskeletal binding serves as an anchor to
localize the iso-2 transporter within the pellicular membrane, and that the flagellar targeting signal of iso-1 diverts this transporter into the flagellar membrane and away from the pellicular microtubules.
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