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SNAP23-Kif5 complex controls mGlu1 receptor trafficking.

Fabrice Raynaud1, Vincent Homburger1, Martial Seveno2

  • 1IGF, CNRS, INSERM, Univ. Montpellier, Montpellier, France.

Journal of Molecular Cell Biology
|May 16, 2018
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Summary
This summary is machine-generated.

The Kif5-SNAP23 complex is crucial for trafficking metabotropic glutamate receptor 1 (mGluR1) along dendrites. This interaction ensures proper mGluR1 cell surface expression in hippocampal neurons.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Metabotropic glutamate receptors (mGluRs) are vital for synaptic transmission in the mammalian brain.
  • Their roles in pathophysiology are significant, yet molecular mechanisms for intracellular transport remain unclear.

Purpose of the Study:

  • To identify molecular motors and adaptor proteins involved in trafficking and membrane localization of group I metabotropic glutamate mGlu1 receptors.
  • To elucidate the functional role of identified proteins in mGluR1 trafficking and cell surface expression.

Main Methods:

  • Proteomic analysis of cultured hippocampal neurons to identify interacting proteins with mGlu1 receptor.
  • Recombination techniques to modulate SNAP23-Kif5 interaction.
  • Fluorescence recovery after cleavage assays to assess receptor cell surface targeting.

Main Results:

  • Synaptosome-associated protein 23 (SNAP23) and kinesin motor Kif5 were identified as interacting proteins with mGlu1 receptor.
  • SNAP23 directly binds the carboxyl terminus of mGlu1 receptor.
  • The Kif5-SNAP23 complex regulates mGlu1 receptor trafficking along microtubules and its cell surface expression.

Conclusions:

  • The Kif5-SNAP23 complex is essential for the proper trafficking and cell surface expression of mGlu1 receptors in dendritic processes.
  • This study reveals key molecular determinants for postsynaptic receptor localization.