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J Cell Sci. 2012 Mar 30; 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, while 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 that 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 may 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. Follow this link:
J Cell Sci. 2012 Mar 30; 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, while 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 that 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 may 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. See the original post: What properties allow molecules such asO2 and CO2 to cross a lipid bilayer without help from membrane proteinsI know that molecules that are lipophilic will pass without the aid of integral proteins or facilitators, but, i wasn't … See original here: What properties allow molecules such asO2 and CO2 to cross a lipid bilayer without help from membrane proteinsI know that molecules that are lipophilic will pass without the aid of integral proteins or facilitators, but, i wasn't … More: integral membrane proteins (e.g. GPCRs, ion channels and membrane-associated proteins) and their complexes with … studies. – Performs hands-on crystallization of membrane proteins using LCP, hanging/sitting/sandwich drop techniques… Read more here: integral membrane proteins (e.g. GPCRs, ion channels and membrane-associated proteins) and their complexes with … studies. – Performs hands-on crystallization of membrane proteins using LCP, hanging/sitting/sandwich drop techniques… Read more here: The winning poster is entitled Structural Investigations of CLC-ec1, A Large Integral Membrane Protein, Using Solution-State NMR and Nanodisc Techology and features Thomas Chew, Sherwin J. Abraham, Shelley M. View original post here: |
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