Skip to main content
Log in

Models for the length distributions of actin filaments: II. Polymerization and fragmentation by gelsolin acting together

  • Published:
Bulletin of Mathematical Biology Aims and scope Submit manuscript

Abstract

In a previous paper, we studied elementary models for polymerization, depolymerization, and fragmentation of actin filaments (Edelstein-Keshet and Ermentrout, 1998, Bull. Math. Biol. 60, 449–475). When these processes act together, more complicated dynamics occur. We concentrate on a particular case study, using the actin-fragmenting protein gelsolin. A set of biological parameter values (drawn from the experimental literature) is used in computer simulations of the kinetics of gelsolin-mediated actin filament fragmentation.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Aizawa, H., K. Sutoh and I. Yahara (1996). Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in dictyostelium. J. Cell Biol. 132, 335–344.

    Article  Google Scholar 

  • Andrè, E., F. Lottspeich, M. Schleicher and A. Noegel (1988). Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains. J. Biol. Chem. 263, 722–727.

    Google Scholar 

  • Vasconcellos, C., P. G. Allen, M. E. Wohl, J. M. Drazen, P. A. Janmey and T. P. Stossel (1994). Reduction in viscosity of cystic fibrosis sputum in vitro by gelsolin. Science 263, 969–971.

    Google Scholar 

  • Barron-Casella, E. A., M. A. Torres, S. W. Scherer, H. H. Q. Heng, L. C. Tsui and J. F. Casella (1995). Sequence analysis and chromosomal localization of human cap Z: Conserved residues within the actin-binding domain may link cap Z to gelsolin/severin and profilin protein families. J. Biol Chem. 270, 21472–21479.

    Google Scholar 

  • Biogen (1996). WWW Press Release, Cambridge, MA, Biogen Announces begining of phase I clinical trial of gelsolin as potential treatment for respiratory diseases. http://www.biogen.com/frame/company/index.html

  • Coppin, C. M. and P. Leavis (1992). Quantitation of liquid-crystaline ordering in F-actin solutions. Biophys J. 63, 794–807.

    Google Scholar 

  • Del Castillo, A. R., S. Lemaire, L. Tchakarov, M. Jeyapragasan, J. Doucet, M. Vitale and J. Trifarö (1990). Chromaffin cell scinderin, a novel calcium-dependent actin filament-severing protein. EMBO J. 9, 43–52.

    Google Scholar 

  • Ditsch, A. and A. Wegner (1994). Nucleation of actin polymerization by gelsolin. Eur. J. Biochem. 224, 223–227.

    Article  Google Scholar 

  • Ditsch, A. and A. Wegner (1995). Two low-affinity Ca++ binding sites of gelsolin that regulate association with actin filaments. Eur. J. Biochem. 229, 512–516.

    Article  Google Scholar 

  • Doi, Y. and C. Frieden (1984). Actin polymerization: The effect of brevin on filament size and rate of polymerization. J. Biol. Chem. 259, 11868–11875.

    Google Scholar 

  • Edelstein-Keshet, L. and G. B. Ermentrout (1998). Models for the length distribution of actin filaments: I. Simple polymerization and fragmentation acting alone. Bull. Math. Biol. 60, 449–475.

    Article  MATH  Google Scholar 

  • Fath, K. R. and D. R. Burgess (1995). Not actin alone. Curr. Biol. 5, 591–593

    Article  Google Scholar 

  • Furuhasi, K. and S. Hatano (1990). Control of actin filament length by phosphorylation of fragmin-actin complex. J. Cell Biol. 111, 1081–1087

    Article  Google Scholar 

  • Hartwig, J. H., D. Brown, D. A. Ausiello, T. P. Stossel and L. Orci (1990). Polarization of gelsolin and actin binding protein in kidney epithelial cells. J. Histochem. Cytochem. 38, 1145–1153.

    Google Scholar 

  • Hartwig, J. H. and D. J. Kwiatkowski (1991). Actin binding proteins. Curr. Opin. Cell Biol. 3, 87–97.

    Article  Google Scholar 

  • Hawkins, M., B. Pope, S. K. Maciver and A. G. Weeds (1993). Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochem. 32, 9985–9993.

    Article  Google Scholar 

  • Hayden, S. M., P. Miller, A. Brauweiler and J. R. Bamburg (1993). Analysis of the interactions of actin depolymerizing factor with G-and F-actin. Biochem. 32, 9994–10004.

    Article  Google Scholar 

  • Horn, R. A. and C. R. Johnson (1985). Matrix Analysis, Cambridge: Cambridge University Press.

    MATH  Google Scholar 

  • Howard, T., C. Chaponnier, H. Yin and T. Stossel (1990). Gelsolin-actin interaction and actin polymerization in human neutrophils. J. Cell Biol. 110, 1983–1991.

    Article  Google Scholar 

  • Janmey, P. A. and P. T. Matsudaira (1988). Functional comparison of vilin and gelsolin. J. Biol. Chem. 263, 16738–16743.

    Google Scholar 

  • Janmey, P. A., J. Peetermans, K. S. Zaner, T. P. Stossel and T. Tanaka (1986). Structure and mobility of actin filaments as measured by quasielectric light scattering, viscometry and electron microscopy. J. Biol. Chem. 261, 8357–8362.

    Google Scholar 

  • Kwiatkowski, D. J. (1988). Predominant induction of gelsolin and actin-binding protein during myeloid differentiation. J. Biol. Chem. 263, 13857–13862.

    Google Scholar 

  • Laham, L. E., J. A. Lamb, P. G. Allen and P. A. Janmey (1993). Selective binding of gelsolin to actin monomers containing ADP. J. Biol. Chem. 268, 14202–14207.

    Google Scholar 

  • Lauffenburger, D. A. and A. F. Horowitz (1996), Cell migration: a physically integrated molecular process. Cell 84, 359–369.

    Article  Google Scholar 

  • Lueck, A., J. D’Haese and H. Hinssen (1995). A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression. Biochem. J. 305, 767–775.

    Google Scholar 

  • Maciver, S. K., H. G. Zot and T. D. Pollard (1991). Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol. 115, 1611–1620.

    Article  Google Scholar 

  • Madden, T. L. and J. Herzfeld (1994). Crowding-induced organization of cytoskeletal elements: II. dissolution of spontaneously formed filament bundles by capping proteins. J. Cell Biol. 126, 169–174.

    Article  Google Scholar 

  • McGough, A. (1997). Structural Studies of Gelsolin: Actin Interactions, Baylor College of Medicine, Houston, http://dali.bcm.tmc.edu/∼amy/Gelsolin.html

    Google Scholar 

  • Mitchison, T. J. and L. Cramer (1996). Actin-based cell motility and cell locomotion. Cell 84, 371–379.

    Article  Google Scholar 

  • Moon, A. and D. G. Drubin (1995). The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics. Mol. Biol. Cell 6, 1423–1431.

    Google Scholar 

  • Redmond, T. and S. H. Zigmond (1993). Distribution of F-actin elongation sites in lysed polymorphonuclear leukocytes parallels the distribution of endogenous F-actin. Cell Motil. Cytoskel. 26, 1–18.

    Article  Google Scholar 

  • Schindl, M., E. Wallraff, B. Deubzer, W. Witke, G. Gerisch and E. Sackmann (1995). Cell-substrate interactions and locomotion of dictyostelium wild-type and mutants defective in three cytoskeletal proteins: a study using quantitative reflection interference contrast microscopy. Biophys. J. 68, 1177–1190.

    Article  Google Scholar 

  • Schnuchel, A., R. Wiltscheck, L. Eichinger, M. Schleicher and T. A. Holak (1995). Structure of severin domain in solution. J. Mol. Biol. 247, 21–27.

    Article  Google Scholar 

  • Schoepper, B. and A. Wegner (1991). Rate constants and equilibrium constants for binding of actin to the 1:1 gelsolin-actin complex. Eur J. Biochem. 202, 1127–1131.

    Article  Google Scholar 

  • Schoepper, B. and A. Wegner (1992). Gelsolin binds to polymeric actin at a low rate. J. Biol. Chem. 267, 13924–13927.

    Google Scholar 

  • Selve, N. and A. Wegner (1986). Rate of treadmilling of actin filaments in vitro. J. Mol. Biol. 187, 627–631.

    Article  Google Scholar 

  • Selve, N. and A. Wegner (1987). pH-dependentrate of formation of the gelsolin-actin complex from gelsolin and monomeric actin. Eur. J. Biochem. 168, 111–115.

    Article  Google Scholar 

  • Stossel, T. P. (1994). Gelsolin: another potential therapy for CF Sputum. http://www.ai.mit.edu/people/mernst/cf/cfri

  • Teubner, A., I. Sobek-Klocke, H. Hinssen and U. Eichenlaub-Ritter (1994). Distribution of gelsolin in mouse ovary. Cell Tissue Research 276, 535–544.

    Google Scholar 

  • Theriot, J. A. (1994). Actin filament dynamics in cell motility, in Actin: Biophysics, Biochemistry, and Cell Biology, J. E. Estes and P. J. Higgins (Eds), New York: Plenum Press, pp. 133–145.

    Google Scholar 

  • Vandekerckhove, J., G. Bauw, K. Vancompernolle, B. Honoré and J. Celis (1990). Comparative two-dimensional gel analysis and microsequencing identifies gelsolin as one of the most prominent downregulated markers of transformed human fibroblast and epithelial cells. J. Cell Biol. 111, 95–102

    Article  Google Scholar 

  • Weber, I., E. Walraff, R. Albrecht and G. Gerisch (1995). Motility and substratum adhesion of dictyostelium wild-type and cytoskeletal mutant cells: a study by RICM/bright-field double-view image analysis. J. Cell Sci. 108, 1519–1530.

    Google Scholar 

  • Yin, H. L., P. A. Janmey and M. Schleicher (1990). Severin is a gelsolin prototype. FEBS Lett. 264, 78–80.

    Article  Google Scholar 

  • Zigmond, S. H. (1993). Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil. Cytoskel. 25, 309–316.

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ermentrout, G.B., Edelstein-Keshet, L. Models for the length distributions of actin filaments: II. Polymerization and fragmentation by gelsolin acting together. Bull. Math. Biol. 60, 477–503 (1998). https://doi.org/10.1006/bulm.1997.0012

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1006/bulm.1997.0012

Keywords

Navigation