Open AccessFunctional role for the class IX myosin myr5 in epithelial cell infection by Shigella flexneri
Author(s) -
Graf Barbara,
Bähler Martin,
Hilpelä Pirta,
Böwe Christian,
Adam Thomas
Publication year - 2000
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1046/j.1462-5822.2000.00084.x
Subject(s) - rhoa , shigella flexneri , biology , myosin , gtpase , cdc42 , microbiology and biotechnology , cytoskeleton , ezrin , actin , internalization , rhoc , cell , signal transduction , escherichia coli , biochemistry , gene
Efficient control of Shigella ‐induced, rho‐dependent cytoskeletal rearrangements seems to be required to shape the delicate cellular structures associated with bacterial invasion of epithelial cells. We therefore studied a class IX myosin and rho antagonist, the GTPase‐activating protein (GAP) myr5, for a potential role in the bacterial entry process. We show that myr5 is recruited into bacterial entry spots. The recruitment pattern resembled that of rhoC or ezrin, but not rhoA, rac or CDC42, while in vitro GAP activity of myr5 was similar for rhoA, B or C. Analysis of myr5 mutants suggested that GTPase‐ or ATP‐binding activites are not required for Shigella ‐induced recruitment of this atypical myosin to the bacterial entry site. Functional studies revealed a potential dual role of the myosin functions and the GAP module of myr5 for bacterial internalization.