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Related Experiment Video

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Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

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Mechanical force and cytoplasmic Ca(2+) activate yeast TRPY1 in parallel.

Zhenwei Su¹, Xinliang Zhou, Stephen H Loukin

¹University of Wisconsin-Madison, 53706, USA.

The Journal of Membrane Biology

|February 17, 2009

Summary

Transient receptor potential (TRP) channels like TRPY1 sense mechanical and osmotic stimuli. This study reveals how calcium ions and membrane stretch interact to control TRPY1 channel gating, uncovering a parallel gating mechanism.

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Area of Science:

Molecular Biology
Biophysics
Cell Biology

Background:

Mechanical and osmotic stimuli sensing is crucial for all life forms.
Transient receptor potential (TRP) ion channels are key players in mechanosensation.
Yeast TRPY1 channel is activated by mechanical force and calcium ions.

Purpose of the Study:

To investigate the interplay between membrane stretch force and cytoplasmic Ca(2+) in TRPY1 channel gating.
To elucidate the structural basis of TRPY1's polymodal activation.

Main Methods:

Patch clamp electrophysiology to measure TRPY1 channel activity.
Site-directed mutagenesis to probe the role of C-terminal domains.
Analysis of Ca(2+) dependence and force-induced activation.

Main Results:

TRPY1 channel can be activated by membrane stretch force independently of Ca(2+).
Cytoplasmic Ca(2+) significantly enhances force-induced channel activity.
A C-terminal negative charge cluster is critical for Ca(2+) potentiation, but not for force activation.

Conclusions:

A structure-function model proposes parallel gating mechanisms for Ca(2+) and membrane stretch.
Ca(2+) binding to the cytoplasmic domain and membrane stretching both generate gating forces.
These forces converge at the channel gate, demonstrating a coordinated activation process.