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

Progress on the structure and function of aquaporin 1

J B Heymann1, P Agre, A Engel

  • 1M. E. Müller-Institute for Microscopic Structural Biology, Biozentrum, University of Basel, Switzerland.

Journal of Structural Biology
|June 6, 1998
PubMed
Summary

Nature created highly specific water channels, like aquaporin-1, essential for cell function. Structural studies reveal their tetrameric complex and transmembrane helices, explaining water transport mechanisms.

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

Conditional progression-free survival in patients with metastatic hormone receptor-positive, human epidermal growth factor receptor 2-negative breast cancer treated with first-line ribociclib and endocrine therapy: real-world data from the RIBANNA study.

ESMO open·2025
Same author

A region within the third extracellular loop of rat Aquaporin 6 precludes trafficking to plasma membrane in a heterologous cell line.

Scientific reports·2021
Same author

MTT Heterogeneity in Perfusion CT Imaging as a Predictor of Outcome after Aneurysmal SAH.

AJNR. American journal of neuroradiology·2021
Same author

Local resolution estimates of cryoEM reconstructions.

Current opinion in structural biology·2020
Same author

Less is more: re-evaluating systematic reviews.

Colorectal disease : the official journal of the Association of Coloproctology of Great Britain and Ireland·2018
Same author

Single equalizer strategy with no information transfer for conflict escalation.

Physical review. E·2018

Area of Science:

  • Biophysics
  • Molecular Biology
  • Cell Physiology

Background:

  • Cells require precise regulation of water transport across membranes.
  • Nature has evolved highly efficient and specific water channels, known as aquaporins.
  • Aquaporin-1, initially found in red blood cells, is related to the Major Intrinsic Protein (MIP) family.

Purpose of the Study:

  • To understand the structural basis of water channel activity.
  • To elucidate the arrangement of transmembrane segments in MIP family proteins.
  • To investigate the mechanism of water permeation through aquaporins.

Main Methods:

  • Three-dimensional electron microscopy at medium resolution.
  • Cloning and sequencing of MIP family proteins.

Related Experiment Videos

  • Sequence analysis and mutagenesis studies.
  • Assignment of electron microscopy densities to predicted protein structures.

    • Main Results:

    • Aquaporins form tetrameric complexes with six tilted transmembrane helices per monomer.
    • Interhelical loops within each monomer form a central pore implicated in water transport.
    • Four conserved polar residues (E142-N192-N76-E17) are proposed as key to the water pathway.

    Conclusions:

    • The structure of aquaporins explains their high water flux and specificity.
    • Understanding aquaporin structure provides insights into transmembrane protein organization.
    • Conserved residues likely play a critical role in facilitating water movement through the channel.