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Cellular microbiology

Two types of tail

Nature Reviews Molecular Cell Biology volume 5, pages 172–173 (2004)Cite this article

Arp2/3 nucleates and polymerizes actin filaments to form the networks of short and highly branched filaments that are found both in lamellipodia (flattened, sheet-like structures that project from cells) and in the actin tails of bacteria such as Listeria sp. However, it is less clear how the long and unbranched filaments that are generated during filopodia formation are made. In this study, Cossart and co-workers focused their attention on R. conorii, which produces an actin tail that is reminiscent of the actin filaments of filopodia.

They searched the genome sequence of R. conorii and identified a protein — RickA — that is structurally similar to known Arp2/3-activating proteins. Although RickA lacks a membrane anchor, the authors found that it is highly expressed on the bacterial cell surface. In addition, they showed that, although RickA alone cannot polymerize actin in vitro, it can activate the Arp2/3 complex to do so.

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References

ORIGINAL RESEARCH PAPER

  1. Gouin, E. et al. The RickA protein of Rickettsia conorii activates the Arp2/3 complex. Nature 427, 457–461 (2004)

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FURTHER READING

  1. Frischknecht, F. & Way, M. Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol. 11, 30–38 (2001)

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Authors
  1. Rachel Smallridge
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Pascale Cossart's laboratory

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Smallridge, R. Two types of tail. Nat Rev Mol Cell Biol 5, 172–173 (2004). https://doi.org/10.1038/nrm1344

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