Skip to main content
PMC home page
Biophysical Journal logoLink to Biophysical Journal
. 1986 Jan;49(1):149–151. doi: 10.1016/S0006-3495(86)83630-X

Mechanism of Actin Filament Self-Assembly and Regulation of the Process by Actin-Binding Proteins

Thomas D Pollard
PMCID: PMC1329614  PMID: 19431625

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bonder E. M., Fishkind D. J., Mooseker M. S. Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell. 1983 Sep;34(2):491–501. doi: 10.1016/0092-8674(83)90382-3. [DOI] [PubMed] [Google Scholar]
  2. Carlier M. F., Pantaloni D., Korn E. D. Evidence for an ATP cap at the ends of actin filaments and its regulation of the F-actin steady state. J Biol Chem. 1984 Aug 25;259(16):9983–9986. [PubMed] [Google Scholar]
  3. Cooper J. A., Blum J. D., Pollard T. D. Acanthamoeba castellanii capping protein: properties, mechanism of action, immunologic cross-reactivity, and localization. J Cell Biol. 1984 Jul;99(1 Pt 1):217–225. doi: 10.1083/jcb.99.1.217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cooper J. A., Buhle E. L., Jr, Walker S. B., Tsong T. Y., Pollard T. D. Kinetic evidence for a monomer activation step in actin polymerization. Biochemistry. 1983 Apr 26;22(9):2193–2202. doi: 10.1021/bi00278a021. [DOI] [PubMed] [Google Scholar]
  5. Frieden C. Actin and tubulin polymerization: the use of kinetic methods to determine mechanism. Annu Rev Biophys Biophys Chem. 1985;14:189–210. doi: 10.1146/annurev.bb.14.060185.001201. [DOI] [PubMed] [Google Scholar]
  6. Frieden C. Polymerization of actin: mechanism of the Mg2+-induced process at pH 8 and 20 degrees C. Proc Natl Acad Sci U S A. 1983 Nov;80(21):6513–6517. doi: 10.1073/pnas.80.21.6513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Frieden C. The Mg2+-induced conformational change in rabbit skeletal muscle G-actin. J Biol Chem. 1982 Mar 25;257(6):2882–2886. [PubMed] [Google Scholar]
  8. Isenberg G., Aebi U., Pollard T. D. An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature. 1980 Dec 4;288(5790):455–459. doi: 10.1038/288455a0. [DOI] [PubMed] [Google Scholar]
  9. Pollard T. D., Cooper J. A. Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry. 1984 Dec 18;23(26):6631–6641. doi: 10.1021/bi00321a054. [DOI] [PubMed] [Google Scholar]
  10. Pollard T. D. Measurement of rate constants for actin filament elongation in solution. Anal Biochem. 1983 Oct 15;134(2):406–412. doi: 10.1016/0003-2697(83)90316-0. [DOI] [PubMed] [Google Scholar]
  11. Pollard T. D., Mooseker M. S. Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores. J Cell Biol. 1981 Mar;88(3):654–659. doi: 10.1083/jcb.88.3.654. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pollard T. D. Polymerization of ADP-actin. J Cell Biol. 1984 Sep;99(3):769–777. doi: 10.1083/jcb.99.3.769. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Pollard T. D. Purification of a calcium-sensitive actin gelation protein from Acanthamoeba. J Biol Chem. 1981 Jul 25;256(14):7666–7670. [PubMed] [Google Scholar]
  14. Pollard T. D. Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins. J Cell Biol. 1984 Dec;99(6):1970–1980. doi: 10.1083/jcb.99.6.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Pollard T. D., Weeds A. G. The rate constant for ATP hydrolysis by polymerized actin. FEBS Lett. 1984 May 7;170(1):94–98. doi: 10.1016/0014-5793(84)81376-9. [DOI] [PubMed] [Google Scholar]
  16. Reichstein E., Korn E. D. Acanthamoeba profilin. A protein of low molecular weight from Acanpthamoeba castellanii that inhibits actin nucleation. J Biol Chem. 1979 Jul 10;254(13):6174–6179. [PubMed] [Google Scholar]
  17. Tobacman L. S., Korn E. D. The kinetics of actin nucleation and polymerization. J Biol Chem. 1983 Mar 10;258(5):3207–3214. [PubMed] [Google Scholar]
  18. Tseng P. C., Runge M. S., Cooper J. A., Williams R. C., Jr, Pollard T. D. Physical, immunochemical, and functional properties of Acanthamoeba profilin. J Cell Biol. 1984 Jan;98(1):214–221. doi: 10.1083/jcb.98.1.214. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wegner A., Engel J. Kinetics of the cooperative association of actin to actin filaments. Biophys Chem. 1975 Jul;3(3):215–225. doi: 10.1016/0301-4622(75)80013-5. [DOI] [PubMed] [Google Scholar]
  20. Wegner A., Savko P. Fragmentation of actin filaments. Biochemistry. 1982 Apr 13;21(8):1909–1913. doi: 10.1021/bi00537a032. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES