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An actin nucleation mechanism mediated by Bni1 and Profilin

Nature Cell Biology volume 4, pages 626–631 (2002)Cite this article

Abstract

Formins are required for cell polarization and cytokinesis, but do not have a defined biochemical activity. In Saccharomyces cerevisiae, formins and the actin-monomer-binding protein profilin are specifically required to assemble linear actin structures called 'actin cables'. These structures seem to be assembled independently of the Arp2/3 complex, the only well characterized cellular mediator of actin nucleation. Here, an activated yeast formin was purified and found to promote the nucleation of actin filaments in vitro. Formin-dependent actin nucleation was stimulated by profilin. Thus, formin and profilin mediate actin nucleation by an Arp2/3-independent mechanism. These findings suggest that distinct actin nucleation mechanisms may underlie the assembly of different actin cytoskeletal structures.

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Figure 1: Bni1-mini is a functional formin truncation.
Figure 2: Bni1-mini promotes the assembly of linear actin filaments in vitro.
Figure 3: Bni1-mini nucleates barbed-end actin polymerization independently of the Arp2/3 complex.
Figure 4: Profilin enhances Bni1-mini-induced actin assembly.

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References

  1. Pollard, T. D., Blanchoin, L. & Mullins, R. D. Annu. Rev. Biophys. Biomol. Struct. 29, 545–576 (2000).

    Article  CAS  PubMed Central  Google Scholar 

  2. Condeelis, J. Trends Cell Biol. 11, 288–293 (2001).

    Article  CAS  Google Scholar 

  3. Higgs, H. N. & Pollard, T. D. Annu. Rev. Biochem. 70, 649–676 (2001).

    Article  CAS  Google Scholar 

  4. Evangelista, M., Pruyne, D., Amberg, D. C., Boone, C. & Bretscher, A. Nature Cell Biol. 4, 32–41 (2002).

    Article  CAS  Google Scholar 

  5. Hudson, A. M. & Cooley, L. J. Cell Biol. 156, 677–687 (2002).

    Article  CAS  PubMed Central  Google Scholar 

  6. Lew, D. J. Nature Cell Biol. 4, E29–E30 (2002).

    Article  CAS  PubMed Central  Google Scholar 

  7. Sagot, I., Klee, S. K. & Pellman, D. Nature Cell Biol. 4, 42–50 (2002).

    Article  CAS  PubMed Central  Google Scholar 

  8. Winter, D. C., Choe, E. Y. & Li, R. Proc. Natl Acad. Sci. USA 96, 7288–7293 (1999).

    Article  CAS  PubMed Central  Google Scholar 

  9. Feierbach, B. & Chang, F. Curr. Biol. 11, 1656–1665 (2001).

    Article  CAS  Google Scholar 

  10. Holt, M. R. & Koffer, A. Trends Cell Biol. 11, 38–46 (2001).

    Article  CAS  Google Scholar 

  11. Haarer, B. K. et al. J. Cell Biol. 110, 105–114 (1990).

    Article  CAS  Google Scholar 

  12. Ozaki-Kuroda, K. et al. Mol. Cell. Biol. 21, 827–839 (2001).

    Article  CAS  PubMed Central  Google Scholar 

  13. Sampath, P. & Pollard, T. D. Biochemistry 30, 1973–1980 (1991).

    Article  CAS  Google Scholar 

  14. MacLean-Fletcher, S. & Pollard, T. D. Cell 20, 329–341 (1980).

    Article  CAS  PubMed Central  Google Scholar 

  15. Pollard, T. D. & Cooper, J. A. Biochemistry 23, 6631–6641 (1984).

    Article  CAS  Google Scholar 

  16. Du, J. & Frieden, C. Biochemistry 37, 13276–13284 (1998).

    Article  CAS  Google Scholar 

  17. Machesky, L. M. et al. Proc. Natl Acad. Sci. USA 96, 3739–3744 (1999).

    Article  CAS  Google Scholar 

  18. Lu, J. & Pollard, T. D. Mol. Biol. Cell 12, 1161–1175 (2001).

    Article  CAS  PubMed Central  Google Scholar 

  19. Wolven, A. K., Belmont, L. D., Mahoney, N. M., Almo, S. C. & Drubin, D. G. J. Cell Biol. 150, 895–904 (2000).

    Article  CAS  PubMed Central  Google Scholar 

  20. Higgs, H. N., Blanchoin, L. & Pollard, T. D. Biochemistry 38, 15212–15222 (1999).

    Article  CAS  Google Scholar 

  21. Pantaloni, D., Boujemaa, R., Didry, D., Gounon, P. & Carlier, M. F. Nature Cell Biol. 2, 385–391 (2000).

    Article  CAS  Google Scholar 

  22. Pruyne, D. et al. Science online (cited 06 June 2002) DOI: 10.1126/science.1072309.

  23. Drenckhahn, D. & Pollard, T. D. J. Biol. Chem. 261, 12754–12758 (1986).

    CAS  PubMed  Google Scholar 

  24. Nakano, K. et al. Mol. Biol. Cell 10, 2481–2491 (1999).

    Article  CAS  PubMed Central  Google Scholar 

  25. Tominaga, T. et al. Mol. Cell 5, 13–25 (2000).

    Article  CAS  PubMed Central  Google Scholar 

  26. Watanabe, N., Kato, T., Fujita, A., Ishizaki, T. & Narumiya, S. Nature Cell Biol. 1, 136–143 (1999).

    Article  CAS  PubMed Central  Google Scholar 

  27. Goode, B. L. et al. J. Cell Biol. 144, 83–98 (1999).

    Article  CAS  PubMed Central  Google Scholar 

  28. Goode, B. L., Rodal, A. A., Barnes, G. & Drubin, D. G. J. Cell Biol. 153, 627–634 (2001).

    Article  CAS  PubMed Central  Google Scholar 

  29. Winter, D., Lechler, T. & Li, R. Curr. Biol. 9, 501–504 (1999).

    Article  CAS  Google Scholar 

  30. Alberts, A. S. J. Biol. Chem. 276, 2824–2830 (2001).

    Article  CAS  PubMed Central  Google Scholar 

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Acknowledgements

We thank H. Balcer, C. Boone, D. Drubin, A. Lasek, and A. Manning for reagents; P. Carvalho, T. Fujiwara, M.E. McLaughlin and T. Rapoport for comments on the manuscript; H. Balcer, P. Carvalho, H. Falet, J. Hartwig and T. Rapoport for discussions. This work was supported by grants from the Pew Scholars Program (B.G.); a Basil O'Connor Scholar Award (B.G.); a pre-doctoral fellowship from the Howard Hughes Medical Institute (A.R.); the National Institutes of Health (GM61345, D.P.); the Leukemia and Lymphoma Society of America (D.P.).

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Authors and Affiliations

  1. Departments of Pediatric Oncology, The Dana-Farber Cancer Institute and Pediatric Hematology, The Children's Hospital, Harvard Medical School, 44 Binney Street, Boston, 02115, MA, USA

    Isabelle Sagot & David Pellman

  2. Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, 94720-3202, CA, USA

    Avital A. Rodal & Bruce L. Goode

  3. Department of Biology, Rosenstiel Medical Center, Brandeis University, 415 South Street, Waltham, 02454, MA, USA

    James Moseley & Bruce L. Goode

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  1. Isabelle Sagot
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Correspondence to Bruce L. Goode or David Pellman.

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Sagot, I., Rodal, A., Moseley, J. et al. An actin nucleation mechanism mediated by Bni1 and Profilin. Nat Cell Biol 4, 626–631 (2002). https://doi.org/10.1038/ncb834

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