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

The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin

Maria K Vartiainen1, Tuija Mustonen, Pieta K Mattila

  • 1Programs in Cellular Biotechnology, Institute of Biotechnology, Viikki Biocenter, University of Helsinki, Helsinki, 00014 Finland.

Molecular Biology of the Cell
|January 26, 2002
PubMed
Summary

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

GlycoAvatars: bead-coated membrane models for studying the cancer-immune cells interactome.

Communications biology·2026
Same author

Mechanisms of CARMIL dimerization, autoinhibition, and capping protein binding.

Science advances·2026
Same author

Stem cell specification and niche formation in developing incisor require actomyosin forces.

Stem cells (Dayton, Ohio)·2025
Same author

Calponin isoforms define the cell-type-specific organization and dynamics of actomyosin bundles.

Current biology : CB·2025
Same author

Lgi2-deficient mice manifest epileptiform activity in the developing hippocampal network and ADHD-like behavioural comorbidity in adulthood.

Experimental neurology·2025
Same author

Gene regulatory mechanisms guiding bifurcation of inhibitory and excitatory neuron lineages in the mouse anterior brainstem.

eLife·2025

Mammalian cells utilize three distinct actin-depolymerizing factor (ADF)/cofilin isoforms, each with unique biochemical properties and expression patterns, to regulate actin filament dynamics in specific cellular contexts.

Area of Science:

  • Cell Biology
  • Biochemistry

Background:

  • Actin-depolymerizing factor (ADF)/cofilins are crucial for regulating actin filament turnover.
  • Multicellular organisms possess multiple ADF/cofilin isoforms, but their functional distinctions are not well understood.

Purpose of the Study:

  • To investigate the biological differences between mammalian ADF/cofilin isoforms.
  • To characterize the expression patterns and biochemical activities of three identified mouse ADF/cofilins.

Main Methods:

  • Northern blot and in situ hybridization were used to analyze gene expression.
  • Biochemical assays were performed to assess actin depolymerization, filament disassembly, and monomer binding affinities.

Main Results:

  • Three ADF/cofilin isoforms (cofilin-1, cofilin-2, and ADF) were identified in mice, with distinct tissue-specific expression patterns.

Related Experiment Videos

  • While all isoforms efficiently depolymerize platelet actin, ADF exhibits the strongest pH-dependent disassembly activity.
  • Cofilin-2 shows higher affinity for ATP-actin monomers and can promote filament assembly, unlike the other isoforms.
  • Conclusions:

    • Distinct biochemical properties and expression profiles suggest specialized roles for each ADF/cofilin isoform in regulating actin dynamics.
    • These findings highlight the evolution of specific ADF/cofilin isoforms to meet the diverse needs of actin regulation across different mammalian cell types.