Cytoskeletal association is important for differential targeting of glucose transporter isoforms in Leishmania

Erik L. Snapp, Scott M. Landfear

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1775-1783
Number of pages9
JournalJournal of Cell Biology
Volume139
Issue number7
DOIs
StatePublished - Dec 29 1997

ASJC Scopus subject areas

  • Cell Biology

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