Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Facilitated Diffusion01:16

Facilitated Diffusion

The plasma membrane, a critical structure in cellular biology, houses an array of transporters, or carrier proteins, interspersed within its lipid bilayer. These proteins play a crucial role in solute transport through facilitated diffusion, a form of passive diffusion that uses transporters to move the molecules across the membrane.
In this process, substrates such as organic compounds and ions interact with a transporter on one side, triggering conformational changes in proteins that enable...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Passive Diffusion: Overview and Kinetics01:17

Passive Diffusion: Overview and Kinetics

Passive diffusion is a critical process that allows small lipophilic drugs to cross the cell membrane along a concentration gradient. This mechanism's efficiency depends on four primary factors: the membrane's surface area, the drug's lipid-water partition coefficient, the concentration gradient, and the membrane's thickness.
When administered orally, drugs establish a substantial concentration gradient between the gastrointestinal (GI) lumen and the bloodstream, expediting their diffusion into...

You might also read

Related Articles

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

Sort by
Same author

Glycolipids slow interfacial proton migration while preserving surface proton retention.

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

6-Ketocholestanol can form micelles in aqueous solution absorbing hydrophobic mitochondrial uncouplers: a case of N-alkylated picramic acid.

Bioelectrochemistry (Amsterdam, Netherlands)·2026
Same author

Evaluating Force Matching as a Parametrization Strategy for the CHARMM36m Force Field Using Phosphorylation.

The journal of physical chemistry. B·2026
Same author

Ionophoric Properties of 1,3-Bis[4-(trifluoromethyl)phenyl]urea on Bilayer Lipid Membranes in the Absence of Fatty Acids.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

A Semi-Quantitative Yeast Complementation Platform for Characterizing Urea and Ammonia Transport by Membrane Channels.

Current protocols·2026
Same author

Classification of Mitochondrial Protonophoric Uncouplers and their Modifications in Biological Environment.

Biochemistry. Biokhimiia·2025

Related Experiment Video

Updated: Jun 24, 2026

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
07:33

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

Coupled diffusion of peripherally bound peptides along the outer and inner membrane leaflets.

Andreas Horner1, Yuri N Antonenko, Peter Pohl

  • 1Institut für Biophysik, Johannes Kepler Universität Linz, Linz, Austria.

Biophysical Journal
|April 8, 2009
PubMed
Summary

Peripheral protein binding across cell membranes can occur without lipid rafts. Charged molecules like poly-lysine (PLL) binding to one membrane leaflet influence the other, suggesting mechanical coupling drives transmembrane signaling.

More Related Videos

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Related Experiment Videos

Last Updated: Jun 24, 2026

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
07:33

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Area of Science:

  • Biophysics
  • Membrane Biology
  • Cell Signaling

Background:

  • Transmembrane signaling requires communication between opposite membrane leaflets.
  • The molecular mechanisms connecting lipid rafts across leaflets remain unclear.
  • Peripheral protein binding is a key aspect of transmembrane signaling.

Purpose of the Study:

  • To investigate how peripheral molecule binding to one membrane leaflet is detected by the opposite leaflet.
  • To elucidate the role of mechanical interactions in interleaflet communication.
  • To determine if lipid rafts are necessary for this communication.

Main Methods:

  • Utilized planar lipid bilayers to model cell membranes.
  • Employed fluorescence correlation spectroscopy to measure molecular diffusion.
  • Studied the binding of charged poly-lysine (PLL) molecules to membrane leaflets.

Main Results:

  • Poly-lysine binding to one leaflet was detected at the opposite leaflet, independent of raft lipids.
  • Lipid diffusion coefficients changed significantly upon PLL binding, indicating nanodomain formation.
  • Interleaflet coupling was primarily driven by mechanical interactions, specifically membrane undulations, rather than electrostriction.

Conclusions:

  • Transmembrane signaling can be mediated by mechanical coupling between membrane leaflets, not solely by lipid rafts.
  • Opposing poly-lysine molecules align to suppress membrane undulations, facilitating interleaflet communication.
  • This mechanical interaction mechanism provides a general model for transmembrane signaling involving membrane-separated ligands.