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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Cation Interactions and Membrane Potential Induce Conformational Changes in NaPi-IIb.

Monica Patti1, Cristina Fenollar-Ferrer2, Andreas Werner3

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|September 8, 2016
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Summary
This summary is machine-generated.

Changes in sodium-coupled phosphate cotransporter structure were revealed using fluorophore labeling. Membrane potential and ion interactions cause significant protein rearrangements, impacting transport function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Transport

Background:

  • Sodium-coupled phosphate cotransporters (SLC34 family) exhibit voltage-dependence due to charge displacement and sodium ion interactions.
  • Previous studies identified key residues at the Na1 site through structural modeling and functional analysis.

Purpose of the Study:

  • To investigate the conformational changes in SLC34A2 protein in response to membrane potential using functional and fluorometric assays.
  • To validate the hypothesis that Na1 site mutations alter protein dynamics and structural rearrangements.

Main Methods:

  • Construction of double mutants of flounder SLC34A2 protein with Na1-site mutations and cysteine substitutions for fluorophore labeling in Xenopus oocytes.
  • Characterization using steady-state, presteady-state, and fluorometric assays, including iodide quenching experiments.
  • Mapping mutations onto a homology model of the flounder protein.

Main Results:

  • Fluorescence intensity changes (ΔF) in response to membrane potential steps were observed at three labeled positions.
  • Altered presteady-state kinetics and changes in the fluorophore microenvironment's voltage dependence and time course corroborated Na1 site perturbation.
  • Iodide quenching revealed membrane potential-dependent aqueous accessibility of the fluorophore microenvironment.

Conclusions:

  • Membrane potential and cation interactions induce significant, large-scale structural rearrangements in SLC34A2 cotransporters.
  • These findings provide compelling evidence linking protein dynamics to transporter function and voltage-dependence.