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

Dynamin at actin tails.

Eunkyung Lee1, Pietro De Camilli

  • 1Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, P.O. Box 9812, New Haven, CT 06536-0812, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 10, 2002
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

Dystrophic changes of nigrostriatal axons harboring a Synj1 Parkinson mutation suggest catastrophic failure of endocytic mechanisms.

bioRxiv : the preprint server for biology·2026
Same author

Cryo-EM structure of soluble VPS13C suggests its regulation by a conformational switch and by calmodulin.

Molecular cell·2026
Same author

Mechanism of lipid transfer by bridge-like protein VPS13A and the scramblase XK.

Cell·2026
Same author

Pharmacokinetics and safety of candidate biosimilar CT-P55 versus reference secukinumab: a three-arm, randomized, double-blinded, single-dose, multicenter, Phase I study.

Expert opinion on investigational drugs·2026
Same author

Inhibition of de novo ceramide synthesis mitigates alpha-synuclein pathology in a Parkinson's disease mouse model.

NPJ Parkinson's disease·2026
Same author

Molecular insights into bulk lipid transport from structural studies of the bridge-like protein VPS13A complexed with the scramblase XKR1.

bioRxiv : the preprint server for biology·2026

Dynamin, a GTPase essential for endocytosis, interacts with the actin cytoskeleton. This study reveals dynamin

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Dynamin is a GTPase crucial for endocytosis, the process cells use to internalize molecules.
  • Previous research suggests a connection between dynamin and the actin cytoskeleton, a key component of cellular structure and movement.
  • Actin dynamics are implicated in endocytosis, making the dynamin-actin link particularly significant.

Purpose of the Study:

  • To investigate the functional relationship between dynamin and the actin cytoskeleton in the context of endocytosis.
  • To determine dynamin's role in actin nucleation and polymerization at cellular membranes.

Main Methods:

  • Localization studies using endogenous dynamin 2 and green fluorescence protein (GFP) fusion proteins of dynamin 1 and 2.
  • Analysis of actin comets and tails induced by Listeria or type I PIP kinase (PIPK) overexpression.

Related Experiment Videos

  • Functional assays using dynamin mutants with alterations in the GTPase and proline-rich domains.

    • Main Results:

    • Dynamin was found to localize to actin comets and was enriched at the interface between actin tails and moving organelles.
    • Dynamin mutants with GTPase domain mutations inhibited actin tail nucleation and reduced their speed.
    • A dynamin mutant lacking the proline-rich domain disrupted actin tail formation and a membrane-associated actin scaffold (podosome rosette).

    Conclusions:

    • Dynamin is part of a protein network that regulates actin nucleation from membranes.
    • Dynamin may link the membrane fission event in endocytosis to actin polymerization, facilitating vesicle separation from the plasma membrane.