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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
Author(s) -
Niebuhr Kirsten,
Ebel Frank,
Frank Ronald,
Reinhard Matthias,
Domann Eugen,
Carl Uwe D.,
Walter Ulrich,
Gertler Frank B.,
Wehland Jürgen,
Chakraborty Trinad
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.17.5433
Subject(s) - biology , listeria monocytogenes , cytoskeleton , microbiology and biotechnology , computational biology , genetics , cell , bacteria
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.