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

Aquaporins01:25

Aquaporins

6.6K
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
6.6K
Pore Transport and Ion-Pair Transport01:17

Pore Transport and Ion-Pair Transport

1.4K
Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited  but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct...
1.4K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.7K
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...
6.7K
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

4.9K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
4.9K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.8K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.8K
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

4.5K
4.5K

You might also read

Related Articles

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

Sort by
Same author

Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins.

International journal of molecular sciences·2024
Same author

The role of phosphorylation in calmodulin-mediated gating of human AQP0.

The Biochemical journal·2023
Same author

Effect of controlled hypotensive hemorrhage on plasma sodium levels in anesthetized pigs: An exploratory study.

Physiological reports·2023
Same author

High-resolution structure of a fish aquaporin reveals a novel extracellular fold.

Life science alliance·2022
Same author

Insight into the Mammalian Aquaporin Interactome.

International journal of molecular sciences·2022
Same author

Ezrin Is a Novel Protein Partner of Aquaporin-5 in Human Salivary Glands and Shows Altered Expression and Cellular Localization in Sjögren's Syndrome.

International journal of molecular sciences·2021

Related Experiment Video

Updated: Feb 20, 2026

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy
08:39

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Published on: December 12, 2025

568

Aquaporin Protein-Protein Interactions.

Jennifer Virginia Roche1, Susanna Törnroth-Horsefield2

  • 1Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Box 124, 221 00 Lund, Sweden. jennifer.roche@biochemistry.lu.se.

International Journal of Molecular Sciences
|October 28, 2017
PubMed
Summary

Aquaporins are water channels regulated by protein interactions. Understanding these interactions reveals how aquaporins function and can lead to new disease treatments.

Keywords:
aquaporingatingmembrane channelmembrane proteinprotein-protein interactionstrafficking

More Related Videos

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies
04:22

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Published on: November 20, 2021

5.0K
Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example
14:20

Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example

Published on: October 8, 2014

16.5K

Related Experiment Videos

Last Updated: Feb 20, 2026

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy
08:39

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy

Published on: December 12, 2025

568
Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies
04:22

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Published on: November 20, 2021

5.0K
Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example
14:20

Measuring the Osmotic Water Permeability Coefficient Pf of Spherical Cells: Isolated Plant Protoplasts as an Example

Published on: October 8, 2014

16.5K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Aquaporins are tetrameric membrane channels crucial for water and solute transport.
  • Their function in eukaryotes is regulated by gating and trafficking.
  • Protein-protein interactions are key to aquaporin regulation and function.

Purpose of the Study:

  • To review recent knowledge on aquaporin protein-protein interactions.
  • To categorize these interactions into three main types.
  • To highlight the structural basis of aquaporin regulation.

Main Methods:

  • Literature review focusing on recent advancements.
  • Categorization of aquaporin interactions: tetramer-tetramer, monomer-monomer (hetero-tetramerization), and transient interactions.
  • Analysis of structural differences enabling specific regulation.

Main Results:

  • Identified three primary modes of aquaporin protein-protein interactions.
  • Highlighted conserved structural features with subtle variations dictating specificity.
  • Emphasized the role of these interactions in organism-, tissue-, and trigger-specific aquaporin regulation.

Conclusions:

  • Detailed understanding of aquaporin interactions is essential for comprehending their physiological roles.
  • Structural insights into aquaporin interactions can guide the development of targeted therapeutics for human diseases.
  • Further research into aquaporin interactions may unlock novel treatment strategies.