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Related Experiment Videos

Comparison between the gelsolin and adseverin domain structure.

T Sakurai1, H Kurokawa, Y Nonomura

  • 1Department of Pharmacology, Faculty of Medicine, University of Tokyo, Japan.

The Journal of Biological Chemistry
|August 25, 1991
PubMed
Summary

Adseverin, a protein regulating actin filaments, has functional domains similar to gelsolin and villin. Its N-terminal fragments bind actin in a calcium-dependent manner, contributing to actin severing.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Adseverin is a 74-kDa protein (scinderin) that modulates actin dynamics.
  • It binds calcium and phospholipids, promoting actin polymerization, filament severing, and barbed end capping.
  • Its N-terminal half retains these actin-binding and severing properties.

Purpose of the Study:

  • To investigate the functional domain structure of adseverin.
  • To identify specific fragments responsible for adseverin's actin-binding and severing activities.
  • To compare adseverin's structure to related actin-binding proteins like gelsolin and villin.

Main Methods:

  • Proteolysis of the N-terminal half of adseverin to generate fragments.
  • Analysis of calcium-dependent binding of fragments to monomeric actin.

Related Experiment Videos

  • Amino acid sequencing of fragments to determine their N-terminal sequences and homology.
  • Assessment of actin filament fragmentation and severing activity of fragments.

    • Main Results:

    • Two N-terminal fragments (Mr 15,000 and 31,000) exhibited Ca(2+)-dependent binding to monomeric actin.
    • The Mr 31,000 fragment demonstrated actin filament fragmentation activity.
    • Severing activity of the Mr 31,000 fragment was inhibited by acidic phospholipids.
    • Amino acid sequencing revealed homology of other fragments to gelsolin and villin.

    Conclusions:

    • Adseverin possesses N-terminal fragments with Ca(2+)-sensitive actin-binding and severing functions.
    • Adseverin shares a functional domain structure with the core regions of gelsolin and villin.
    • These findings elucidate the molecular mechanisms underlying adseverin's role in actin regulation.