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Related Experiment Videos

Conformational changes in actin induced by its interaction with gelsolin

S Khaitlina1, H Hinssen

  • 1Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.

Biophysical Journal
|August 1, 1997
PubMed
Summary

Gelsolin binding induces conformational changes in ECP-actin, enabling polymerization nucleation despite Ca2+ binding. These changes in actin structure, particularly in subdomain 2 and the C-terminus, are crucial for actin-gelsolin interactions and filament formation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Dynamics

Background:

  • Actin polymerization is essential for cell structure and motility.
  • Gelsolin is a key regulator of actin dynamics, involved in filament nucleation and severing.
  • Proteolytic cleavage of actin can alter its polymerization properties.

Purpose of the Study:

  • To investigate the conformational changes in protease-cleaved actin (ECP-actin) upon binding with gelsolin.
  • To understand how these conformational changes influence actin polymerization and nucleation.
  • To elucidate the role of specific actin domains in actin-gelsolin interactions.

Main Methods:

  • Limited proteolysis using ECP and subtilisin.
  • Gel filtration and fluorometry to assess binding affinities.

Related Experiment Videos

  • Cross-linking experiments with N,N-phenylene-bismaleimide.
  • Analysis of ECP-actin polymerization with Ca2+ and Mg2+.

    • Main Results:

    • ECP-actin, non-polymerizable with Ca2+, forms a stoichiometric complex with gelsolin.
    • This complex acts as a nucleus for intact actin polymerization, indicating a gelsolin-induced conformational change.
    • Binding of ECP-actin to gelsolin is weaker than intact actin, suggesting conformational changes in subdomain 2.
    • Gelsolin binding alters actin conformation in the DNase I-binding loop and stabilizes the C-terminal region.

    Conclusions:

    • Gelsolin binding induces significant conformational changes in ECP-actin, restoring its ability to interact with other actin monomers.
    • Conformational alterations in actin's subdomain 2 and C-terminus are critical for gelsolin-mediated nucleation.
    • These findings provide insights into the molecular mechanisms of actin regulation by gelsolin.