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 Experiment Videos

Junction-forming aquaporins.

Andreas Engel1, Yoshinori Fujiyoshi, Tamir Gonen

  • 1Maurice E. Mueller Institute, University of Basel, Biozentrum, Klingelberstrasse 70, CH-4056 Basel, Switzerland.

Current Opinion in Structural Biology
|January 16, 2008
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Membrane protein structure and dynamics probed by MicroED.

Biochemical Society transactions·2026
Same author

pH-mediated activation of the lysosomal arginine sensor SLC38A9.

FEBS letters·2026
Same author

Rapid Structural Analysis of Natural Products Using MicroED.

Small (Weinheim an der Bergstrasse, Germany)·2026
Same author

Characterization of German SF<sub>6</sub> Emissions.

ACS ES&T air·2025
Same author

Conformational Trajectory of the Molecular Chameleon Grazoprevir From Formulation to Target-Bound.

Chemistry (Weinheim an der Bergstrasse, Germany)·2025
Same author

Discovery of Oxyacanthine Dihydrochloride Monohydrate Polymorphs from Obfuscated Samples by Microcrystal Electron Diffraction.

ChemMedChem·2025
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

Aquaporins (AQPs) are water channels that also mediate cell adhesion. This review highlights AQP0 and AQP4 structures and their roles in cell junction formation and adhesion.

Area of Science:

  • Membrane Biology
  • Biophysics
  • Cellular Physiology

Background:

  • Aquaporins (AQPs) are integral membrane proteins facilitating water and solute transport.
  • Specific aquaporins, notably AQP0 and AQP4, are implicated in cellular adhesion beyond their transport functions.

Purpose of the Study:

  • To review the structural and mechanistic aspects of membrane junctions formed by AQP0 and AQP4.
  • To consolidate evidence supporting the role of AQP0 and AQP4 in cell adhesion.

Main Methods:

  • Analysis of recently determined structures of AQP0 and AQP4 mediated membrane junctions.
  • Review of studies investigating the regulation of junction formation.
  • Synthesis of experimental evidence for AQP0 and AQP4's role in cell adhesion.

Related Experiment Videos

Main Results:

  • Recent structural data reveals how AQP0 and AQP4 form specific membrane junctions.
  • Mechanisms regulating the assembly and disassembly of these junctions have been elucidated.
  • Evidence strongly suggests that AQP0 and AQP4 actively participate in cell-cell adhesion.

Conclusions:

  • AQP0 and AQP4 function as dual-role proteins, acting as both water channels and mediators of cell adhesion.
  • Understanding the structural basis of AQP-mediated junctions is key to deciphering their adhesive functions.
  • Further research into AQP0 and AQP4's adhesive roles may reveal new therapeutic targets for adhesion-related disorders.