Both sequence and context are important for flagellar targeting of a glucose transporter

Khoa D. Tran, Dayana Rodriguez-Contreras, Ujwal Shinde, Scott M. Landfear

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Many of the cilia- and flagella-specific integral membrane proteins identified to date function to sense the extracellular milieu, and there is considerable interest in defining pathways for targeting such proteins to these sensory organelles. The flagellar glucose transporter of Leishmania mexicana, LmxGT1, is targeted selectively to the flagellar membrane, whereas two other isoforms, LmxGT2 and LmxGT3, are targeted to the pellicular plasma membrane of the cell body. To define the flagellar targeting signal, deletions and point mutations were generated in the N-terminal hydrophilic domain of LmxGT1, which mediates flagellar localization. Three amino acids, N95-P96-M97, serve critical roles in flagellar targeting, resulting in strong mistargeting phenotypes when mutagenized. However, to facilitate flagellar targeting of other non-flagellar membrane proteins, it was necessary to attach a larger region surrounding the NPM motif containing amino acids 81-113. Molecular modeling suggests that this region might present the critical NPM residues at the surface of the N-terminal domain. It is likely that the NPM motif is recognized by currently unknown protein-binding partners that mediate flagellar targeting of membrane-associated proteins.

Original languageEnglish (US)
Pages (from-to)3293-3298
Number of pages6
JournalJournal of Cell Science
Volume125
Issue number14
DOIs
StatePublished - Jul 15 2012

Keywords

  • Conformational epitope
  • Flagellar glucose transporter
  • Flagellar-targeting motif
  • Flagellar/ciliary targeting
  • Molecular modeling

ASJC Scopus subject areas

  • Cell Biology

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