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

Utrophin, like its homologue dystrophin, forms a link between the actin cytoskeleton and the extracellular matrix. We have used a new method of image analysis to reconstruct actin filaments decorated with the actin-binding domain of utrophin, which contains two calponin homology domains. We find two different modes of binding, with either one or two calponin-homology (CH) domains bound per actin subunit, and these modes are also distinguishable by their very different effects on F-actin rigidity. Both modes involve an extended conformation of the CH domains, as predicted by a previous crystal structure. The separation of these two modes has been largely dependent upon the use of our new approach to reconstruction of helical filaments. When existing information about tropomyosin, myosin, actin-depolymerizing factor, and nebulin is considered, these results suggest that many actin-binding proteins may have multiple binding sites on F-actin. The cell may use the modular CH domains found in the spectrin superfamily of actin-binding proteins to bind actin in manifold ways, allowing for complexity to arise from the interactions of a relatively few simple modules with actin.

Bibliography

Galkin, V. E., Orlova, A., VanLoock, M. S., Rybakova, I. N., Ervasti, J. M., & Egelman, E. H. (2002). The utrophin actin-binding domain binds F-actin in two different modes. The Journal of Cell Biology, 157(2), 243–251.

Authors 6
  1. Vitold E. Galkin (first)
  2. Albina Orlova (additional)
  3. Margaret S. VanLoock (additional)
  4. Inna N. Rybakova (additional)
  5. James M. Ervasti (additional)
  6. Edward H. Egelman (additional)
References 38 Referenced 72
  1. 10.1006/jmbi.1996.0602 / J. Mol. Biol. (1996)
  2. 10.1006/jmbi.2001.4897 / J. Mol. Biol. (2001)
  3. 10.1016/0022-2836(89)90249-0 / J. Mol. Biol. (1989)
  4. 10.1021/bi00105a021 / Biochemistry (1991)
  5. 10.1021/bi00121a036 / Biochemistry. (1992)
  6. 10.1038/217130a0 / Nature. (1968)
  7. 10.1016/S0304-3991(00)00062-0 / Ultramicroscopy. (2000)
  8. 10.1038/nsb0901-735 / Nat. Struct. Biol. (2001)
  9. 10.1016/S0960-9822(01)00615-7 / Curr. Biol. (2001)
  10. 10.1038/298131a0 / Nature. (1982)
  11. 10.1083/jcb.153.1.75 / J. Cell Biol. (2001)
  12. 10.1038/nsb0997-708 / Nat. Struct. Biol. (1997)
  13. 10.1083/jcb.139.2.387 / J. Cell Biol. (1997)
  14. 10.1038/1828 / Nat. Struct. Biol. (1998)
  15. 10.1083/jcb.200105079 / J. Cell Biol. (2001)
  16. 10.1021/bi961159k / Biochemistry. (1996)
  17. 10.1038/347044a0 / Nature. (1990)
  18. 10.1038/347037a0 / Nature. (1990)
  19. 10.1016/S0969-2126(00)88344-6 / Struct. Fold. Des. (1999)
  20. 10.1006/jmbi.2000.4080 / J. Mol. Biol. (2000)
  21. 10.1016/S0960-9822(02)00678-4 / Curr. Biol. (2002)
  22. 10.1038/364685a0 / Nature. (1993)
  23. 10.1002/1097-0169(200006)46:2<116::AID-CM4>3.0.CO;2-L / Cell Motil. Cytoskel. (2000)
  24. 10.1006/jmbi.2000.3583 / J. Mol. Biol. (2000)
  25. 10.1016/S0969-2126(00)00132-5 / Struct. Fold. Des. (2000)
  26. 10.1006/jmbi.1993.1393 / J. Mol. Biol. (1993)
  27. 10.1016/S0006-3495(94)80791-X / Biophys. J. (1994)
  28. 10.1006/jmbi.2001.4945 / J. Mol. Biol. (2001)
  29. 10.1126/science.1059700 / Science. (2001)
  30. 10.1038/365810a0 / Nature. (1993)
  31. 10.1038/4033 / Nat. Med. (1998)
  32. 10.1038/35092500 / Nature. (2001)
  33. 10.1042/bst0240497 / Biochem. Soc. Trans. (1996)
  34. 10.1242/jcs.108.1.63 / J. Cell Sci. (1995)
  35. 10.1006/jmbi.2001.5025 / J. Mol. Biol. (2001)
  36. 10.1006/jmbi.2000.5213 / J. Mol. Biol. (2001)
  37. 10.1073/pnas.111005398 / Proc. Natl. Acad. Sci. USA. (2001)
  38. 10.1002/(SICI)1097-4644(20000601)77:3<418::AID-JCB7>3.0.CO;2-Z / J. Cell. Biochem. (2000)
Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 12:48 p.m.)
Deposited 2 years, 1 month ago (July 22, 2023, 9:32 a.m.)
Indexed 1 month, 3 weeks ago (July 7, 2025, 2:27 a.m.)
Issued 23 years, 4 months ago (April 15, 2002)
Published 23 years, 4 months ago (April 15, 2002)
Published Online 23 years, 4 months ago (April 15, 2002)
Published Print 23 years, 4 months ago (April 15, 2002)
Funders 0

None

@article{Galkin_2002, title={The utrophin actin-binding domain binds F-actin in two different modes}, volume={157}, ISSN={0021-9525}, url={http://dx.doi.org/10.1083/jcb.200111097}, DOI={10.1083/jcb.200111097}, number={2}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Galkin, Vitold E. and Orlova, Albina and VanLoock, Margaret S. and Rybakova, Inna N. and Ervasti, James M. and Egelman, Edward H.}, year={2002}, month=apr, pages={243–251} }