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

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

8.7K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.7K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.4K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.4K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.1K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.1K
Fluid Mosaic Model01:19

Fluid Mosaic Model

12.3K
Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
12.3K
Membrane Fluidity01:23

Membrane Fluidity

154.7K
Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
154.7K
Lipids as Anchors01:32

Lipids as Anchors

5.7K
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
5.7K

You might also read

Related Articles

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

Sort by
Same author

Anomalous Fluorescence Dynamics Emerge in Densely Labeled Virus-Like Particles.

ACS nano·2026
Same author

Unique Microswitches Positioned Extracellular to the Orthosteric Binding Site Initiate Activation in the β<sub>1</sub>-Adrenergic Receptor.

Journal of chemical information and modeling·2026
Same author

Specificity and Promiscuity of Phosphoinositide Lipid Interactions with the Serotonin<sub>1A</sub> Receptor: Insights from Submillisecond Coarse-Grain Simulations.

ACS chemical neuroscience·2026
Same author

Mechanistic principles of antimicrobial peptides uncovered by charge density-based machine learning.

Chemical communications (Cambridge, England)·2026
Same author

Computational biophysical characterization of a superradiant virus-like particle in its ground state.

bioRxiv : the preprint server for biology·2025
Same author

A Molecular View of Lipid Nanoparticles: Insights into their Morphology and Structural Plasticity.

Small (Weinheim an der Bergstrasse, Germany)·2025

Related Experiment Video

Updated: Aug 26, 2025

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

9.5K

Cofilin-Membrane Interactions: Electrostatic Effects in Phosphoinositide Lipid Binding.

Shikha Prakash1, Anjali Krishna1,2, Durba Sengupta1

  • 1CSIR - National Chemical Laboratory, Dr. Homi Bhabha Road, Pune, 411008, India.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
|October 6, 2022
PubMed
Summary

Cofilin-1 protein preferentially interacts with phosphoinositide lipids (PIP2 and PIP3) in cell membranes. These specific protein-lipid interactions, driven by electrostatics and geometry, influence membrane curvature and lipid organization.

Keywords:
complex membranelipid clusteringmartini coarse-grain simulationsmolecular dynamics simulationsprotein-lipid interactions

More Related Videos

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

9.6K
Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

8.6K

Related Experiment Videos

Last Updated: Aug 26, 2025

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

9.5K
Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

9.6K
Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

8.6K

Area of Science:

  • Molecular Biophysics
  • Cell Biology
  • Computational Biology

Background:

  • The actin cytoskeleton is crucial for cell structure and dynamics, interacting with the cell membrane via actin-binding proteins.
  • Cofilin-1 is a key actin-binding protein, but its specific interactions with membrane lipids remain poorly understood.
  • Understanding these interactions is vital for elucidating cofilin-1's role in cellular processes.

Purpose of the Study:

  • To investigate the molecular mechanisms and specificity of cofilin-1 interactions with membrane lipids.
  • To analyze the role of protein-lipid interactions in cofilin-1's association with the cell membrane.

Main Methods:

  • Coarse-grain molecular dynamics simulations were employed to model cofilin-1 in complex lipid bilayers.
  • Analysis focused on identifying specific protein-lipid interaction sites and their contribution to binding specificity.
  • Control simulations were conducted to dissect the roles of electrostatics and geometry in lipid binding.

Main Results:

  • Cofilin-1 exhibited maximal interaction with phosphoinositide (PIP) lipids, particularly PIP2 and PIP3.
  • Simulations identified specific cofilin-1 residues involved in PIP lipid binding, consistent with experimental data.
  • PIP lipid clustering induced lipid demixing and persistent membrane curvature around the bound protein.

Conclusions:

  • Electrostatic and geometric factors are critical for the specificity of cofilin-1 binding to PIP lipids.
  • The study provides insights into the physico-chemical basis of cofilin-1-PIP lipid interactions.
  • Findings contribute to a deeper understanding of cofilin-1's membrane association and its functional implications.