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

A gelsolin-like Ca2+-dependent actin-binding domain in villin.

P Matsudaira, R Jakes, J E Walker

    Nature
    |May 16, 1985
    PubMed
    Summary

    Villin, an actin-binding protein, bundles actin filaments at low calcium levels but severs them at high calcium concentrations. A purified villin fragment shows calcium-dependent actin-severing activity, suggesting shared mechanisms with gelsolin.

    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

    Comparison of a Nerve Gas Detoxifying Enzyme from Squid and from Pseudomonas diminuta.

    The Biological bulletin·2017
    Same author

    A PHYSICO-CHEMICAL STUDY OF THE MECHANICAL PROPERTIES OF LOW AND INTERMEDIATE MOISTURE FOODS.

    Journal of texture studies·2017
    Same author

    A Commensal Strain of Staphylococcus epidermidis Overexpresses Membrane Proteins Associated with Pathogenesis When Grown in Biofilms.

    The Journal of membrane biology·2015
    Same author

    Nucleotide sequences of the genes for the alpha, beta and epsilon subunits of wheat chloroplast ATP synthase.

    Plant molecular biology·2013
    Same author

    Mitochondrial nucleoid interacting proteins support mitochondrial protein synthesis.

    Nucleic acids research·2012
    Same author

    Human C4orf14 interacts with the mitochondrial nucleoid and is involved in the biogenesis of the small mitochondrial ribosomal subunit.

    Nucleic acids research·2012

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Villin is an actin-binding protein crucial for microfilament organization in intestinal brush border microvilli.
    • Villin exhibits dual functionality: bundling actin filaments at physiological calcium concentrations (<1 µM) and severing them at higher concentrations (>1 µM).

    Purpose of the Study:

    • To investigate the molecular mechanisms underlying villin's actin-binding and calcium-dependent regulatory activities.
    • To identify specific actin-binding domains within villin responsible for its severing and bundling functions.

    Main Methods:

    • Purification of a 44,000-Mr villin fragment.
    • Preliminary biochemical characterization of the purified fragment.
    • Partial amino-acid sequencing of the villin fragment.

    Main Results:

    • A 44,000-Mr villin fragment was successfully purified.
    • This fragment demonstrated calcium-dependent actin-severing activity.
    • Amino-terminal sequencing revealed homology to gelsolin, another actin-severing protein.

    Conclusions:

    • The identified villin fragment possesses calcium-regulated actin-severing properties.
    • Sequence homology suggests a shared structural basis and evolutionary relationship between villin and gelsolin.
    • Further research into these domains will elucidate the molecular details of actin filament regulation by villin.

    Related Experiment Videos