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

Structure of Cadherins01:25

Structure of Cadherins

3.6K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
3.6K
Structure of Porins01:21

Structure of Porins

3.2K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.2K
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

7.2K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
7.2K
COP Coated Vesicles00:59

COP Coated Vesicles

8.0K
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
8.0K
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

3.2K
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...
3.2K
Conserved Binding Sites01:49

Conserved Binding Sites

4.4K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.4K

You might also read

Related Articles

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

Sort by
Same author

OpenGerminal: an open-source implementation of the Germinal antibody design pipeline.

bioRxiv : the preprint server for biology·2026
Same author

Protein-enhanced small molecule disruptors of ordered membrane domains.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Conformational landscape and ligand-dependent clustering of the human type 2 IP<sub>3</sub> receptor.

Nature communications·2026
Same author

Structure-guided compound prioritization strategy for virtual screening identifies putative binders for the nuclear receptor LRH-1.

bioRxiv : the preprint server for biology·2026
Same author

Profiling the CFTR Variant Selectivity and Off-Target Interactions of VX-121.

bioRxiv : the preprint server for biology·2026
Same author

Contributions of conserved and species-specific CagX (VirB9) domains to the assembly and function of the <i>Helicobacter pylori</i> Cag type IV secretion system.

Infection and immunity·2026

Related Experiment Video

Updated: Sep 12, 2025

Production and Optimization of LTE, a Leishmania tarentolae Derived Cell-Free Protein Expression System for Recombinant Protein Production
03:59

Production and Optimization of LTE, a Leishmania tarentolae Derived Cell-Free Protein Expression System for Recombinant Protein Production

Published on: November 8, 2024

1.2K

Evolutionarily diverse caveolins share a common structural framework built around amphipathic disks.

Bing Han1,2, Sarah M Connolly3, Darrin T Schultz4

  • 1Center for Membrane and Cell Physiology, University of Virginia , Charlottesville, VA, USA.

The Journal of Cell Biology
|August 7, 2025
PubMed
Summary

Caveolins, ancient proteins predating animals, share a conserved structure. This study reveals their ancient framework and disk assembly, offering new insights into their function across diverse species.

More Related Videos

A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
07:47

A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters

Published on: April 20, 2015

9.9K
Expression and Purification of Mammalian Bestrophin Ion Channels
08:12

Expression and Purification of Mammalian Bestrophin Ion Channels

Published on: August 2, 2018

8.4K

Related Experiment Videos

Last Updated: Sep 12, 2025

Production and Optimization of LTE, a Leishmania tarentolae Derived Cell-Free Protein Expression System for Recombinant Protein Production
03:59

Production and Optimization of LTE, a Leishmania tarentolae Derived Cell-Free Protein Expression System for Recombinant Protein Production

Published on: November 8, 2024

1.2K
A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
07:47

A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters

Published on: April 20, 2015

9.9K
Expression and Purification of Mammalian Bestrophin Ion Channels
08:12

Expression and Purification of Mammalian Bestrophin Ion Channels

Published on: August 2, 2018

8.4K

Area of Science:

  • Evolutionary biology
  • Structural biology
  • Cell biology

Background:

  • Caveolins are membrane remodeling proteins found across animals, forming caveolae in vertebrates.
  • The structural basis of caveolin function across diverse animal species is not well understood.
  • Human caveolin-1 forms a specific amphipathic disk structure.

Purpose of the Study:

  • To predict and analyze the structures of caveolins across animal diversity.
  • To investigate the evolutionary history and conserved structural elements of caveolins.
  • To establish a structural paradigm for caveolin function in various lineages.

Main Methods:

  • Bioinformatic structure prediction for 73 caveolins and one choanoflagellate caveolin.
  • Comparative structural analysis to identify conserved elements.
  • Cryo-electron microscopy (Cryo-EM) to determine structures of selected caveolins.
  • Chromosomal evolutionary history tracing.

Main Results:

  • Identified seven conserved structural elements in caveolins.
  • Predicted caveolins assemble into amphipathic disks, similar to human caveolin-1.
  • Cryo-EM structures of choanoflagellate and sea urchin caveolins showed high similarity to human caveolin-1.
  • Revealed an ancient chromosomal origin for caveolins predating Metazoa.

Conclusions:

  • Caveolins possess an ancient structural framework that predates the emergence of multicellular animals (Metazoa).
  • The conserved amphipathic disk structure provides a foundation for understanding caveolin function across evolutionary lineages.
  • This study establishes a new structural paradigm for exploring caveolin biology in diverse organisms.