• 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 384: HTS Automated Patch Clamp

    SyncroPatch 384: 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

Buffer Solution

Buffer Solution

2021 - A mechanistic switch from selective transporter to an ion channel impairs the filamentation signalling capability of ammonium transceptors in yeast

 Icon N1   SURFE2R N1 pre-print publication in bioRxiv (2021)

Authors:
Williamson G., Brito A. S., Bizior A., Tamburrino G., Mirandela G. D., Harris T., Hoskisson P. A., Zachariae U., Marini A. M., Boeckstaens M., Javelle A.

Journal:

bioRxiv (2021) doi:10.1101/2021.08.25.457613


Abstract: 

Ammonium translocation through biological membranes by the ubiquitous Amt-Mep-Rh family of transporters plays a key role in all domains of life. Two highly conserved histidine residues protrude into the lumen of these transporters, forming the family’s characteristic Twin-His motif. It has been hypothesized that the motif is essential to confer the selectivity of the transport mechanism. Here, using a combination of in vitro electrophysiology, in vivo yeast functional complementation and in silico molecular dynamics simulations, we demonstrate that variations in the Twin-His motif trigger a mechanistic switch between a specific transporter, depending on ammonium deprotonation, to an unspecific ion channel activity. We therefore propose that there is no selective filter that governs the specificity in Amt-Mep transporters but the inherent mechanism of translocation, dependent on the fragmentation of the substrate, ensures the high specificity of the translocation. We further show that both mechanisms coexist in fungal Mep2 Twin-His variants, disrupting the transceptor function and so inhibiting the filamentation process. These data strongly support a transport mechanism-mediated signalling process in the long-standing debate on the sensory function of Mep2-like transporters.


Download here

Back

Nanion コーポレートブログ

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.