Crossref journal-article
Rockefeller University Press
The Journal of Cell Biology (291)
Abstract

Actin dynamics provide the driving force for many cellular processes including motility and endocytosis. Among the central cytoskeletal regulators are actin-depolymerizing factor (ADF)/cofilin, which depolymerizes actin filaments, and twinfilin, which sequesters actin monomers and caps filament barbed ends. Both interact with actin through an ADF homology (ADF-H) domain, which is also found in several other actin-binding proteins. However, in the absence of an atomic structure for the ADF-H domain in complex with actin, the mechanism by which these proteins interact with actin has remained unknown. Here, we present the crystal structure of twinfilin's C-terminal ADF-H domain in complex with an actin monomer. This domain binds between actin subdomains 1 and 3 through an interface that is conserved among ADF-H domain proteins. Based on this structure, we suggest a mechanism by which ADF/cofilin and twinfilin inhibit nucleotide exchange of actin monomers and present a model for how ADF/cofilin induces filament depolymerization by weakening intrafilament interactions.

Bibliography

Paavilainen, V. O., Oksanen, E., Goldman, A., & Lappalainen, P. (2008). Structure of the actin-depolymerizing factor homology domain in complex with actin. The Journal of Cell Biology, 182(1), 51–59.

Authors 4
  1. Ville O. Paavilainen (first)
  2. Esko Oksanen (additional)
  3. Adrian Goldman (additional)
  4. Pekka Lappalainen (additional)
References 45 Referenced 145
  1. 10.1016/j.molcel.2006.08.006 / Mol. Cell. (2006)
  2. 10.1146/annurev.cellbio.15.1.185 / Annu. Rev. Cell Dev. Biol. (1999)
  3. 10.1016/S0022-2836(02)01008-2 / J. Mol. Biol. (2002)
  4. 10.1038/sj.emboj.7600280 / EMBO J. (2004)
  5. 10.1083/jcb.136.6.1307 / J. Cell Biol. (1997)
  6. 10.1006/jmbi.2002.5438 / J. Mol. Biol. (2002)
  7. 10.1073/pnas.0507021102 / Proc. Natl. Acad. Sci. USA. (2005)
  8. 10.1016/j.bbapap.2006.06.017 / Biochim. Biophys. Acta. (2006)
  9. 10.1002/cm.970260302 / Cell Motil. Cytoskeleton. (1993)
  10. 10.1016/j.tibs.2004.09.004 / Trends Biochem. Sci. (2004)
  11. 10.1038/sj.emboj.7600310 / EMBO J. (2004)
  12. 10.1038/nsb0597-366 / Nat. Struct. Biol. (1997)
  13. 10.1083/jcb.153.1.75 / J. Cell Biol. (2001)
  14. 10.1083/jcb.200308144 / J. Cell Biol. (2003)
  15. 10.1016/j.jmb.2007.12.073 / J. Mol. Biol. (2008)
  16. 10.1021/bi0121104 / Biochemistry. (2002)
  17. 10.1038/sj.emboj.7601019 / EMBO J. (2006)
  18. 10.1016/j.febslet.2004.08.068 / FEBS Lett. (2004)
  19. 10.1016/S0092-8674(04)00403-9 / Cell. (2004)
  20. 10.1038/347044a0 / Nature. (1990)
  21. 10.1038/nature02005 / Nature. (2003)
  22. 10.1161/01.RES.0000237662.23539.0b / Circ. Res. (2006)
  23. 10.1038/nrm1940 / Nat. Rev. Mol. Cell Biol. (2006)
  24. 10.1073/pnas.0611283104 / Proc. Natl. Acad. Sci. USA. (2007)
  25. 10.1107/S0907444995016477 / Acta Crystallogr. D Biol. Crystallogr. (1996)
  26. 10.1093/emboj/16.18.5520 / EMBO J. (1997)
  27. 10.1107/S0021889807021206 / Journal of Applied Crystallography. (2007)
  28. 10.1083/jcb.138.4.771 / J. Cell Biol. (1997)
  29. 10.1038/364685a0 / Nature. (1993)
  30. 10.1242/jcs.02860 / J. Cell Sci. (2006)
  31. 10.1016/j.jmb.2004.08.010 / J. Mol. Biol. (2004)
  32. 10.1091/mbc.e02-03-0157 / Mol. Biol. Cell. (2002)
  33. 10.1083/jcb.200703092 / J. Cell Biol. (2007)
  34. 10.1126/science.1059700 / Science. (2001)
  35. 10.1074/jbc.M208225200 / J. Biol. Chem. (2002)
  36. 10.1016/j.tcb.2004.05.002 / Trends Cell Biol. (2004)
  37. 10.1073/pnas.0608725104 / Proc. Natl. Acad. Sci. USA. (2007)
  38. 10.1016/S0092-8674(03)00120-X / Cell. (2003)
  39. 10.1091/mbc.e05-01-0059 / Mol. Biol. Cell. (2005)
  40. 10.1016/S0021-9258(19)84105-4 / J. Biol. Chem. (2006)
  41. 10.1016/j.jmb.2007.10.076 / J. Mol. Biol. (2008)
  42. 10.1038/365810a0 / Nature. (1993)
  43. 10.1021/bi00367a068 / Biochemistry. (1986)
  44. 10.1016/j.tcb.2004.07.003 / Trends Cell Biol. (2004)
  45. 10.1006/jmbi.1998.2048 / J. Mol. Biol. (1998)
Dates
Type When
Created 17 years, 1 month ago (July 14, 2008, 11:23 p.m.)
Deposited 2 years, 1 month ago (July 21, 2023, 10:41 p.m.)
Indexed 1 month, 1 week ago (July 26, 2025, 5:35 a.m.)
Issued 17 years, 1 month ago (July 14, 2008)
Published 17 years, 1 month ago (July 14, 2008)
Published Online 17 years, 1 month ago (July 14, 2008)
Published Print 17 years, 1 month ago (July 14, 2008)
Funders 0

None

@article{Paavilainen_2008, title={Structure of the actin-depolymerizing factor homology domain in complex with actin}, volume={182}, ISSN={0021-9525}, url={http://dx.doi.org/10.1083/jcb.200803100}, DOI={10.1083/jcb.200803100}, number={1}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Paavilainen, Ville O. and Oksanen, Esko and Goldman, Adrian and Lappalainen, Pekka}, year={2008}, month=jul, pages={51–59} }