Skip to main content

Actin-Gelsolin Interaction

  • Chapter
Actin

Abstract

Gelsolin is an actin-polymerization-regulating protein that has been isolated from many types of cells.1,2 Gelsolin affects actin polymerization in different ways. Gelsolin can fragment actin filaments. Gelsolin binds to the barbed ends of the fragmented actin filaments. The pointed ends of actin filaments remain free for depolymerization and polymerization. Gelsolin nucleates actin filaments to polymerize towards the pointed ends. Furthermore, gelsolin forms complexes with one or two actin molecules. These gelsolin-actin complexes lose the ability to fragment actin filaments. They cap actin filaments by binding to the barbed ends to inhibit polymerization and depolymerization of these ends (Fig. 1).1–4 These interactions of gelsolin with actin filaments are mainly regulated by the second messengers calcium and phosphatidyl inositol phosphates.1–5 Because of the versatility of regulation and interactions with actin and because of its ubiquity in eukaryotic cells gelsolin has attracted our interest. We investigated the equilibrium and the rates of various interactions of gelsolin with actin filaments.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. H. L. Yin and T. P. Stossel, Control of Cytoplasmic Actin Gel-Sol Transformation by Gelsolin, a Calcium-Dependent Regulatory Protein, Nature 281: 583 (1979).

    Article  PubMed  CAS  Google Scholar 

  2. R. Norberg, R. Thorstensson, G. Utter and A. Fagraeus, F-Actin-Depolymerizing Activity of Human Serum, Eur. J. Biochem. 100: 575 (1979).

    Article  PubMed  CAS  Google Scholar 

  3. H. E. Harris and A. G. Weeds, Plasma Actin Depolymerizing Factor Has both Calcium-Dependent and Calcium-Independent Effects on Actin, Biochemistry 22: 2728 (1983).

    Article  PubMed  CAS  Google Scholar 

  4. J. Bryan and M. C. Kurth, Actin-Gelsolin-Interactions: Evidence for Two Actin-Binding Sites, J. Biol. Chem. 259: 7480 (1984).

    PubMed  CAS  Google Scholar 

  5. P. A. Janmey and T. P. Stossel, Modulation of Gelsolin Function by Phosphatidyl 4,5-Bisphosphate, Nature 325: 362 (1987).

    Article  PubMed  CAS  Google Scholar 

  6. N. Selve and A. Wegner, pH-dependent Rate of Formation of the Gelsolin-Actin Complex from Gelsolin and Monomelic Actin, Eur. J. Biochem. 168: 111 (1987).

    Article  PubMed  CAS  Google Scholar 

  7. B. Schoepper and A. Wegner, Rate Constants and Equilibrium Constants for Binding of Actin to the 1: 1 Gelsolin-Actin Complex, Eur. J. Biochem. 202: 1127 (1991).

    Article  PubMed  CAS  Google Scholar 

  8. M. Wille, I. Just, A. Wegner, and K. Aktories, ADP-Ribosylation of Gelsolin-Actin Complexes by Clostridial Toxins, J. Biol. Chem. 267: 50 (1992).

    PubMed  CAS  Google Scholar 

  9. B. Schoepper and A. Wegner, Gelsolin Binds to Polymeric Actin at a Low Rate, J. Biol. Chem. 267: 13924 (1992).

    PubMed  CAS  Google Scholar 

  10. N. Selve and A. Wegner, Rate Constant for Capping of the Barbed Ends of Actin Filaments by the Gelsolin-Actin Complex, Eur. J. Biochem. 155: 397 (1986).

    Article  PubMed  CAS  Google Scholar 

  11. N. Selve and A. Wegner, Rate Constants and Equilibrium Constants for Binding of the Gelsolin-Actin Complex to the Barbed Ends of Actin Filaments in the Presence and Absence of Calcium, Eur. J. Biochem. 160: 379 (1986).

    Article  PubMed  CAS  Google Scholar 

  12. K. Aktories, M. Bärmann, I. Ohishi, S. Tsuyama, K. H. Jakobs and E. Habermann, Botulinum C2 Toxin ADP-ribosylates Actin, Nature 322: 390 (1986).

    Article  PubMed  CAS  Google Scholar 

  13. J. Vandekerckhove, B. Schering, M. Bärmann and K. Aktories, Botulinum C2 Toxin ADP-ribosylates Cytoplasmic ß/γ-Actin in Arginine 177, J. Biol. Chem. 263: 696 (1988).

    PubMed  CAS  Google Scholar 

  14. A. Wegner and K. Aktories, ADP-ribosylated Actin Caps the Barbed Ends of Actin Filaments, J. Biol. Chem. 263: 13739 (1988).

    PubMed  CAS  Google Scholar 

  15. B. Pope, M. Way and A. G. Weeds, Two of the Three Actin-Binding Domains of Gelsolin Bind to the Same Subdomaion of Actin: Implications for Capping and Severing Mechanisms, FEBS Lett. 280: 70 (1991).

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1994 Springer Science+Business Media New York

About this chapter

Cite this chapter

Wegner, A. et al. (1994). Actin-Gelsolin Interaction. In: Estes, J.E., Higgins, P.J. (eds) Actin. Advances in Experimental Medicine and Biology, vol 358. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2578-3_9

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-2578-3_9

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6102-2

  • Online ISBN: 978-1-4615-2578-3

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics