Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Mechanically-gated Ion Channels

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...

Voltage-gated Ion Channels

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several...

Non-gated Ion Channels

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism....

Electrochemical Gradient and Channel Proteins: An Overview

Electrochemical Gradient and Channel Proteins: An Overview

An electrochemical gradient is a fundamental concept in biology and chemistry. It regulates the movement of ions across cell membranes. This movement is influenced by two factors:
The electrical gradient: The electrical gradient across cell membranes refers to the difference in electric charge between the inside and outside of a cell. This difference drives the movement of ions towards or away from the cells. For instance, if the inside of the cell is more negatively charged relative to...

Ion Channels

Ion Channels

The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Structural basis of membrane engagement and polyreactivity control in HIV-1 MPER broadly neutralizing antibodies.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Vaccination elicits HIV broadly neutralizing antibodies in primates.

Nature·2026

Same author

Translating Innovation to Clinic: End-to-End Bioprocess Development and cGMP Manufacturing of N332-GT5 HIV Vaccine Candidate for First-in-Human Trials HVTN144.

bioRxiv : the preprint server for biology·2026

Same author

The SLC15A4-LAMTOR1 interaction licenses endolysosomal TLR-mediated mTOR signaling and inflammatory cytokine production.

bioRxiv : the preprint server for biology·2026

Same author

mRNA delivery of a class 1/4 SARS-CoV-2 neutralizing antibody protects against diverse sarbecoviruses in a lethal mouse challenge model.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Substrate and target selectivity of 4'-fluoroadenosine against viral and host polymerases.

bioRxiv : the preprint server for biology·2026

Search research articles

Related Experiment Video

Updated: Oct 3, 2025

A Behavioral Assay for Mechanosensation of MARCM-based Clones in Drosophila melanogaster

A Behavioral Assay for Mechanosensation of MARCM-based Clones in Drosophila melanogaster

Published on: December 30, 2015

Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1.

Sebastian Jojoa-Cruz¹, Kei Saotome^1,2,3, Che Chun Alex Tsui^1,4

¹Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA, 92037, USA.

Nature Communications

|February 15, 2022

Summary

Flycatcher1 (FLYC1) is a novel mechanosensitive ion channel. Structural studies reveal unique features regulating its gating, crucial for Venus flytrap prey recognition.

More Related Videos

Electrophysiological Method for Whole-cell Voltage Clamp Recordings from Drosophila Photoreceptors

Electrophysiological Method for Whole-cell Voltage Clamp Recordings from Drosophila Photoreceptors

Published on: June 13, 2017

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Related Experiment Videos

Last Updated: Oct 3, 2025

A Behavioral Assay for Mechanosensation of MARCM-based Clones in Drosophila melanogaster

A Behavioral Assay for Mechanosensation of MARCM-based Clones in Drosophila melanogaster

Published on: December 30, 2015

Electrophysiological Method for Whole-cell Voltage Clamp Recordings from Drosophila Photoreceptors

Electrophysiological Method for Whole-cell Voltage Clamp Recordings from Drosophila Photoreceptors

Published on: June 13, 2017

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Area of Science:

Biophysics
Structural Biology
Ion Channel Physiology

Background:

Flycatcher1 (FLYC1) is a candidate mechanosensitive ion channel.
It is implicated in Venus flytrap prey recognition.
FLYC1 is a MscS homolog with unique structural characteristics.

Purpose of the Study:

To characterize the structure and function of FLYC1.
To understand the molecular mechanisms of FLYC1 mechanosensitivity.
To identify structural features regulating ion conduction and gating.

Main Methods:

Cryo-electron microscopy (cryo-EM) for structural determination.
Molecular dynamics (MD) simulations to analyze channel behavior.
Electrophysiology to assess channel function and conductance.

Main Results:

FLYC1 possesses side portals in its cytoplasmic cage, similar to MscS and MSL1 channels, which modulate ion selectivity and conduction.
Unique cytoplasmic flanking regions exhibit 'up' or 'down' conformations, leading to channel asymmetry.
Disrupting an 'up' conformation interaction significantly slows channel deactivation, indicating stabilization of the open state.

Conclusions:

FLYC1 exhibits novel structural features, including asymmetric cytoplasmic regions and regulatory side portals.
Conformational transitions in FLYC1 are critical for its mechanosensitive gating.
These findings provide insights into the regulation of mechanosensation in Venus flytraps.