• Nanion Technologies: イオンチャネル研究のスマートツール

    Nanion Technologies: イオンチャネル研究のスマートツール

  • SyncroPatch 384i: HTS Automated Patch Clamp

    SyncroPatch 384i: HTS Automated Patch Clamp

  • SURFE²R 96SE: ラベルフリーのトランスポーターHTS

    SURFE²R 96SE: ラベルフリーのトランスポーターHTS

  • Dynamic Clamp: Patchliner

    Dynamic Clamp: Patchliner

  • 脂質二分子膜実験: Orbitシリーズ

    脂質二分子膜実験: Orbitシリーズ

  • CardioExcyte 96 SOL: 心筋の光ペーシング

    CardioExcyte 96 SOL: 心筋の光ペーシング

Our Product Portfolio

SyncroPatch 384

SyncroPatch 384

Patchliner

Patchliner

Port-a-Patch

Port-a-Patch

Port-a-Patch mini

Port-a-Patch mini

CardioExcyte 96

CardioExcyte 96

FLEXcyte 96

FLEXcyte 96

SURFE²R 96SE

SURFE²R 96SE

SURFE²R N1

SURFE²R N1

Orbit 16 TC

Orbit 16 TC

Orbit Mini

Orbit Mini

Vesicle Prep Pro

Vesicle Prep Pro

2021 - Gating the channel pore of ionotropic glutamate receptors with bacterial substrate binding proteins

 icon pap  Port-a-Patch prepublication in bioRxiv (2021)

Authors:
Bernhard M., Laube B.

Journal:

bioRxiv (2021) doi: 10.1101/2021.01.27.428399


Abstract: 

Tetrameric ionotropic glutamate receptors (iGluRs) mediate excitatory neurotransmission in the mammalian central nervous system and are involved in learning, memory formation, and pathological processes. Based on structural and sequence similarities of the ligand-binding and channel domains of iGluR subunits to bacterial binding proteins and potassium channels, iGluRs are thought to have originally arisen from their fusion. Here we report the functional coupling of the bacterial ectoine binding protein EhuB to the channel pore-forming transmembrane domains of the bacterial GluR0 receptor by stabilization of dimeric binding domains. Insertion of a disulfide bridge in the dimer interface abolished desensitization of the channel current analogous to mammalian iGluRs. These results demonstrate the functional compatibility of bacterial binding proteins to the gate of the channel pore of an iGluR. Moreover, our results highlight the modular structure and crucial role of binding domain dimerization in the functional evolution of iGluRs.


Download here.

Back

We use cookies on our website. Some of them are essential for the operation of the site, while others help us to improve this site and the user experience (tracking cookies). You can decide for yourself whether you want to allow cookies or not. Please note that if you reject them, you may not be able to use all the functionalities of the site.