Protein modification fine-tunes the cell’s force producers

Lappalainen, Pekka

doi:10.1038/d41586-018-07882-0

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09 January 2019

Protein modification fine-tunes the cell’s force producers

Identification of the enzyme that catalyses a site-specific modification of the protein actin reveals how this change modulates the function of the cell’s force-producing machinery.

Pekka Lappalainen⁰

Pekka Lappalainen
1. Pekka Lappalainen is in the HiLIFE Institute of Biotechnology, University of Helsinki, Helsinki 00014, Finland.
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Actin is one of the most abundant proteins in our cells. It assembles into filaments that produce force for many processes that are essential to the life of animals, plants and fungi — including cell migration and division, and muscle contraction¹. The organization and dynamics of actin filaments in cells are regulated by a large array of actin-binding proteins. Moreover, post-translational modifications of actin — the addition of certain chemical groups to its amino-acid residues, or their removal — is thought to have a role in controlling the cellular functions of actin filaments. However, the proteins that catalyse these changes have been elusive. Writing in Nature, Wilkinson et al.² report the identification of the long-sought enzyme that catalyses the methylation (addition of a methyl group) of actin, and shed light on the biological role of this post-translational modification in animals.

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Nature 565, 297-298 (2019)

doi: https://doi.org/10.1038/d41586-018-07882-0

References

Pollard, T. D. & Cooper, J. A. Science 326, 1208–1212 (2009).
Article PubMed Google Scholar
Wilkinson, A. W. et al. Nature 565, 372–376 (2019).
Article Google Scholar
Terman, J. R. & Kashina, A. Curr. Opin. Cell Biol. 25, 30–38 (2013).
Article PubMed Google Scholar
Drazic, A. et al. Proc. Natl Acad. Sci. USA 115, 4399–4404 (2018).
Article PubMed Google Scholar
Wiame, E. et al. FEBS J. 285, 3299–3316 (2018).
Article PubMed Google Scholar
Johnson, P., Harris, C. I. & Perry, S. V. Biochem. J. 105, 361–370 (1967).
Article PubMed Google Scholar
Kwiatkowski, S. et al. eLife 7, e37921 (2018).
Article PubMed Google Scholar
Eom, G. H. et al. J. Biol. Chem. 286, 34733–34742 (2011).
Article PubMed Google Scholar
Nyman, T. et al. J. Mol. Biol. 317, 577–589 (2002).
Article PubMed Google Scholar
Yao, X., Grade, S., Wriggers, W. & Rubenstein, P. A. J. Biol. Chem. 274, 37443–37449 (1999).
Article PubMed Google Scholar
Kotila, T. et al. Nature Commun. 9, 1892 (2018).
Article PubMed Google Scholar
Blanchoin, L., Pollard, T. D. & Mullins, R. D. Curr Biol. 10, 1273–1282 (2000).
Article PubMed Google Scholar