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

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.7K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.7K

You might also read

Related Articles

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

Sort by
Same author

Deep Immunophenotyping Reveals Distinct Immune Signatures in Axial Spondyloarthritis and Psoriatic Arthritis.

Arthritis & rheumatology (Hoboken, N.J.)·2026
Same author

Covariate selection and adjustment for efficacy and safety endpoints in indirect comparative effectiveness analyses of CAR-T-cell therapies for large B-cell lymphoma: a systematic review.

Journal of comparative effectiveness research·2026
Same author

DGAT-driven futile lipid cycling has a pronounced, yet concealed, thermogenic function.

Cell metabolism·2026
Same author

Suggested experimental design and computational modeling to infer single-cell lipid dynamics from a single destructive measurement.

iScience·2026
Same author

Alkyne lipids as tracers of lipid metabolism.

Methods in enzymology·2026
Same author

Cholesterol-lowering effects of oats induced by microbially produced phenolic metabolites in metabolic syndrome: a randomized controlled trial.

Nature communications·2026

Related Experiment Video

Updated: Mar 1, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

7.2K

Structure-function analysis of human stomatin: A mutation study.

Stefanie Rungaldier1, Ellen Umlauf2, Mario Mairhofer1

  • 1Department of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, Vienna, Austria.

Plos One
|June 3, 2017
PubMed
Summary
This summary is machine-generated.

Stomatin, a cholesterol-binding protein, requires specific domains for membrane association and oligomerization. Its C-terminus influences mobility and actin cytoskeleton binding.

More Related Videos

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

18.0K
In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila
06:41

In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila

Published on: August 20, 2019

14.4K

Related Experiment Videos

Last Updated: Mar 1, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

7.2K
Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

18.0K
In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila
06:41

In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila

Published on: August 20, 2019

14.4K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Stomatin is an ancient, oligomeric, monotopic membrane protein found in cholesterol-rich lipid rafts.
  • It belongs to the SPFH superfamily, sharing features with proteins like caveolins.
  • Recent structural studies identified key residues and subdomains crucial for stomatin's function.

Purpose of the Study:

  • To investigate the functional significance of specific amino acid residues and domains within stomatin.
  • To elucidate the roles of these domains in cholesterol binding, membrane association, oligomerization, and cytoskeletal interactions.

Main Methods:

  • Site-directed mutagenesis (exchanges and deletions) of stomatin domains.
  • Expression of GFP-tagged stomatin mutants.
  • Analysis of subcellular localization, molecular dynamics, and biochemical properties.
  • Fluorescence Recovery After Photobleaching (FRAP) for lateral mobility studies.

Main Results:

  • Stomatin directly binds cholesterol.
  • At least two distinct domains are essential for associating with cholesterol-rich membranes.
  • The coiled-coil domain is critical for stomatin oligomerization.
  • Membrane association also contributes to oligomer formation.
  • The C-terminus is the primary determinant of lateral mobility and cortical actin binding.

Conclusions:

  • Stomatin's structure-function relationship is dependent on specific domains, particularly for cholesterol interaction and membrane localization.
  • Oligomerization is influenced by both intrinsic domain properties and membrane environment.
  • The C-terminus plays a key role in stomatin's dynamic behavior and interaction with the cytoskeleton.