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

Structural basis for budding by the ESCRT-III factor CHMP3.

Tadeusz Muzioł1, Estela Pineda-Molina, Raimond B Ravelli

  • 1European Molecular Biology Laboratory, 6 rue Jules Horowitz, 38042 Grenoble, France.

Developmental Cell
|June 3, 2006
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

Improving the anticancer efficacy of azole-platinum(II) complexes through a Pluronic® micelle formulation strategy.

Dalton transactions (Cambridge, England : 2003)·2026
Same author

Antibody-mediated targeting of SOSIP HIV-1 Env to skin Langerhans cells potentiates humoral responses.

EBioMedicine·2026
Same author

Lack of evidence for cargo release of CD63-EVs into recipient cells.

Scientific reports·2026
Same author

Synthesis of New Volatile Derivatives of Biogenic Amines, Carbamates for Analytical Applications.

Materials (Basel, Switzerland)·2026
Same author

Protocol for HIV-1 budding control by inducible inhibition of ESCRT-III.

STAR protocols·2025
Same author

The ectodomain sheddase ADAM10 restricts HIV-1 propagation and is counteracted by Nef.

Science advances·2025

Researchers determined the crystal structure of human CHMP3, revealing how it forms lattices on membranes. This structure is key to understanding viral budding and cellular processes like multivesicular body biogenesis.

Area of Science:

  • Structural Biology
  • Cell Biology
  • Virology

Background:

  • The vacuolar protein sorting (VPS) machinery, specifically ESCRT-III proteins, is essential for multivesicular body (MVB) biogenesis.
  • Enveloped viruses hijack the VPS machinery, including ESCRT-III, to facilitate their budding and release from host cells.

Purpose of the Study:

  • To elucidate the molecular architecture of the human ESCRT-III protein, CHMP3, through its crystal structure.
  • To understand the assembly mechanism of CHMP3 and its role in membrane budding, particularly in the context of viral replication (e.g., HIV-1).

Main Methods:

  • Determined the crystal structure of human CHMP3 to 2.8 Å resolution.
  • Investigated CHMP3 assembly through dimerization modes and lattice formation.
  • Utilized in vivo assays with CHMP3 mutants and fusion proteins to assess bilayer interaction and viral budding inhibition.

Related Experiment Videos

Main Results:

  • The crystal structure reveals CHMP3 adopts a flat helical arrangement that self-assembles into a lattice.
  • CHMP3 utilizes distinct dimerization modes to form the lattice, exposing a basic surface for membrane interaction.
  • Mutations in basic and dimerization regions impair membrane binding and rescue dominant-negative effects on HIV-1 budding.

Conclusions:

  • CHMP3 polymerization and lattice formation on membranes, mediated by specific bilayer-recognizing surfaces, are crucial for the final stages of viral budding.
  • These findings suggest a conserved mechanism of membrane remodeling by CHMP proteins across different cellular functions and viral systems.