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Enteropathogenic E. coli acts through WASP and Arp2/3 complex to form actin pedestals

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Figure 1: WASP is recruited through its GTPase-binding domain (GBD) to EPEC pedestals.
Figure 2: Pedestal formation and localization of Arp2/3c to pedestals require the WASP acidic domain.


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The authors thank A. Mallavarapu and J. Taunton for helpful discussions, S. Keshavarzi for assistance, M. Welch for Arp2/3c antibodies, H.Miki for N-WASP cDNA, and H. Bourne, A. Johnson and J. Engel for commenting on the manuscript. The work was supported by the H.H.M.I. (O.D.W and B.B.F.), the N.S.E.R.C., Canada (D.L.G), and grants from the M.R.C., Canada (B.B.F), from the N.I.H. (J.W.S. and A.A.), and from the N.C.I. (J.M.B.).

Correspondence and requests for materials should be addressed to D.K.

Supplementary information is available on Nature Cell Biology’s World-Wide Web site ( or as paper copy from the London editorial office of Nature Cell Biology.

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Correspondence to Daniel Kalman.

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Kalman, D., Weiner, O., Goosney, D. et al. Enteropathogenic E. coli acts through WASP and Arp2/3 complex to form actin pedestals. Nat Cell Biol 1, 389–391 (1999).

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