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

Structure, function, and regulation of myosin 1C.

Barbara Barylko1, Gwanghyun Jung, Joseph P Albanesi

  • 1Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, USA. Barbara.Barylko@utsouthwestern.edu

Acta Biochimica Polonica
|June 4, 2005
PubMed
Summary

Myosin 1C, a motor protein, binds tightly to cell membranes via its neck and tail domains. This binding is crucial for its function, but specific docking proteins may still be needed for precise cellular targeting.

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

Fluorescence Intensity of Protein Tags Is Dependent on Their Subcellular Location.

Cells·2026
Same author

Regulation of actin dynamics by phosphoinositides: Focus on postsynaptic plasticity.

Biochimica et biophysica acta. Molecular and cell biology of lipids·2026
Same author

Effect of Pathogenic Mutations on the Formation of High-Order Dynamin 2 Assemblies in Living Cells.

Biochemistry·2024
Same author

Identification of the GABARAP binding determinant in PI4K2A.

Bioscience reports·2024
Same author

Analysis of Arc/Arg3.1 Oligomerization In Vitro and in Living Cells.

International journal of molecular sciences·2024
Same author

Mimicking Protein Kinase C Phosphorylation Inhibits Arc/Arg3.1 Palmitoylation and Its Interaction with Nucleic Acids.

International journal of molecular sciences·2024

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Motors

Background:

  • Myosin 1C is a mammalian single-headed myosin involved in membrane transport.
  • It comprises motor, neck, and tail domains, with eight human myosin I isoforms existing.
  • Myosin 1C plays a role in translocating plasma membrane channels and transporters.

Purpose of the Study:

  • To investigate the binding mechanisms of Myosin 1C to cell membranes.
  • To understand the role of calcium ions and lipids in Myosin 1C membrane association.
  • To explore the necessity of docking proteins for Myosin 1C subcellular localization.

Main Methods:

  • Biochemical characterization of Myosin 1C domains.
  • Analysis of calmodulin and lipid interactions with Myosin 1C.

Related Experiment Videos

  • Investigation of calcium ion effects on binding properties.

    • Main Results:

    • The neck domain of Myosin 1C exhibits calcium-dependent calmodulin binding.
    • Release of calmodulin exposes lipid-binding sites, particularly for phosphoinositides.
    • Both neck and tail domains contribute to strong, potentially irreversible, membrane association.

    Conclusions:

    • Myosin 1C's membrane binding is regulated by calcium and lipid interactions.
    • Irreversible membrane association occurs when both neck and tail binding sites are engaged.
    • The role of specific docking proteins in Myosin 1C targeting remains an active research area.