Loading…

A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family

The ActA protein of the intracellular pathogen Listeria monocytogenes induces a dramatic reorganization of the actin‐based cytoskeleton. Two profilin binding proteins, VASP and Mena, are the only cellular proteins known so far to bind directly to ActA. This interaction is mediated by a conserved mod...

Full description

Saved in:
Bibliographic Details
Published in:The EMBO journal 1997-09, Vol.16 (17), p.5433-5444
Main Authors: Niebuhr, Kirsten, Ebel, Frank, Frank, Ronald, Reinhard, Matthias, Domann, Eugen, Carl, Uwe D., Walter, Ulrich, Gertler, Frank B., Wehland, Jürgen, Chakraborty, Trinad
Format: Article
Language:English
Subjects:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The ActA protein of the intracellular pathogen Listeria monocytogenes induces a dramatic reorganization of the actin‐based cytoskeleton. Two profilin binding proteins, VASP and Mena, are the only cellular proteins known so far to bind directly to ActA. This interaction is mediated by a conserved module, the EVH1 domain. We identify E/DFPPPPXD/E, a motif repeated 4‐fold within the primary sequence of ActA, as the core of the consensus ligand for EVH1 domains. This motif is also present and functional in at least two cellular proteins, zyxin and vinculin, which are in this respect major eukaryotic analogs of ActA. The functional importance of the novel protein–protein interaction was examined in the Listeria system. Removal of EVH1 binding sites on ActA reduces bacterial motility and strongly attenuates Listeria virulence. Taken together we demonstrate that ActA–EVH1 binding is a paradigm for a novel class of eukaryotic protein–protein interactions involving a proline‐rich ligand that is clearly different from those described for SH3 and WW/WWP domains. This class of interactions appears to be of general importance for processes dependent on rapid actin remodeling.
ISSN:0261-4189
1460-2075
1460-2075
DOI:10.1093/emboj/16.17.5433