Related Experiment Video
Updated: May 17, 2026

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
Published on: June 15, 2018
Modulation of plant TPC channels by polyunsaturated fatty acids
Paul Vijay Kanth Gutla1, Anna Boccaccio, Alexis De Angeli
1Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via De Marini 6, 16149 Genova, Italy.
Abstract:
Polyunsaturated fatty acids (PUFAs) are powerful modulators of several animal ion channels. It is shown here that PUFAs strongly affect the activity of the Slow Vacuolar (SV) channel encoded by the plant TPC1 gene. The patch-clamp technique was applied to isolated vacuoles from carrot taproots and Arabidopsis thaliana mesophyll cells and arachidonic acid (AA) was chosen as a model molecule for PUFAs. Our study was extended to different PUFAs including the endogenous alpha-linolenic acid (ALA). The addition of micromolar concentrations of AA reversibly inhibited the SV channel decreasing the maximum open probability and shifting the half activation voltage to positive values. Comparing the effects of different PUFAs, it was found that the length of the lipophilic acyl chain, the number of double bonds and the polar head were critical for channel modulation.The experimental data can be reproduced by a simple three-state model, in which PUFAs do not interact directly with the voltage sensors but affect the voltage-independent transition that leads the channel from the open state to the closed configuration. The results indicate that lipids play an important role in co-ordinating ion channel activities similar to what is known from animal cells.
Related Concept Videos
Cell Signaling in Plants
Responses to Heat and Cold Stress
C4 Pathway and CAM
C4 Pathway
The C4 pathway is used by plants such as...
Photoreceptors and Plant Responses to Light
Protein Transport to the Inner Chloroplast Membrane
Protein Transport to the Outer Chloroplast Membrane
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.

