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

Cell Polarization by Rho Proteins01:21

Cell Polarization by Rho Proteins

2.7K
Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
2.7K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.3K
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...
2.3K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.0K
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...
3.0K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

5.3K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.3K
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

2.5K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
2.5K
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

7.2K
Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
7.2K

You might also read

Related Articles

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

Sort by
Same author

KRAS Inhibitor Induced Cancer Cell Death Enhances Sensitivity to Immune-Mediated Bystander Killing of Drug-Resistant Subclones.

Cancer research·2026
Same author

A long-chain heparan sulfate capture mechanism directs paracrine GDNF-GFRα1 signalling through RET.

bioRxiv : the preprint server for biology·2026
Same author

Discovery of a sulfotyrosine-motif in the human TrkB extracellular domain required for agonist activation.

bioRxiv : the preprint server for biology·2026
Same author

Cell cycle oscillations in a polarity network facilitate state switching by morphogenetic cues.

Science advances·2026
Same author

Molecular Simulations of Phase Separation in Elastic Polymer Networks.

The journal of physical chemistry. B·2026
Same author

RET receptor tyrosine kinase architecture, assemblies, and activation.

Endocrine-related cancer·2026
Same journal

Scalable phosphotyrosine enrichment with SH2 superbinder enables deep profiling of EGF responses.

The EMBO journal·2026
Same journal

Essential nucleus-apical pole linkage maintains division fidelity during Plasmodium progeny formation.

The EMBO journal·2026
Same journal

From cell atlases to mechanisms: bridging scRNA-seq discovery with in vivo genetics.

The EMBO journal·2026
Same journal

Mitochondrial calcium regulates lipid metabolism by modulating tethering of mitochondria to lipid droplets.

The EMBO journal·2026
Same journal

Chromosome condensation mechanically primes the nucleus for mitosis.

The EMBO journal·2026
Same journal

NDR kinase SAX-1 controls dendrite branch-specific elimination during neuronal remodeling in C. elegans.

The EMBO journal·2026
See all related articles

Related Experiment Video

Updated: Jun 23, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

13.2K

Optimized PAR-2 RING dimerization mediates cooperative and selective membrane binding for robust cell polarity.

Tom Bland1,2, Nisha Hirani1, David C Briggs1

  • 1Francis Crick Institute, London, NW1 1AT, UK.

The EMBO Journal
|June 21, 2024
PubMed
Summary
This summary is machine-generated.

Cell polarity relies on protein dimerization, like PAR-2, for robust yet responsive cell polarization. Optimized dimerization ensures dynamic membrane targeting and feedback, crucial for cellular development.

Keywords:
C. elegans ZygoteCell PolarityPAR ProteinsRING Domain DimerizationSelf-organization

More Related Videos

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analy
12:15

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analy

Published on: October 3, 2017

13.4K
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.2K

Related Experiment Videos

Last Updated: Jun 23, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

13.2K
The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analy
12:15

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analy

Published on: October 3, 2017

13.4K
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.2K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Cell polarity is essential for development and requires finely tuned feedback circuits.
  • Quantitative features of these circuits dictate robustness and responsiveness to cellular cues.
  • The PAR polarity network serves as a model for understanding these regulatory mechanisms.

Purpose of the Study:

  • To investigate the role of PAR-2 protein dimerization in regulating cell polarity.
  • To determine how dimerization affinity impacts the dynamics and robustness of the PAR polarity network.
  • To explore the potential of optimizing oligomerization kinetics for intracellular targeting.

Main Methods:

  • Theoretical modeling of feedback circuits.
  • Experimental analysis of PAR-2 dimerization using its N-terminal RING domain.
  • Quantitative assessment of PAR-2 binding to the plasma membrane.

Main Results:

  • PAR-2 dimerization via its RING domain optimizes binding affinity for dynamic and cooperative membrane localization.
  • Reduced dimerization impairs positive feedback and polarization robustness.
  • Enhanced dimerization leads to kinetic trapping and reduced responsiveness to upstream kinases.

Conclusions:

  • Dynamically oligomeric protein domains, such as the PAR-2 RING domain, are critical for balancing robustness and responsiveness in cell polarity networks.
  • Optimizing dimerization kinetics is a key strategy for achieving dynamic and cooperative intracellular targeting.
  • This study provides insights into the molecular mechanisms underlying cell polarity regulation.