Open AccessFormin‐mediated actin polymerization promotes S almonella invasion
Author(s) -
Truong Dorothy,
Brabant Danielle,
Bashkurov Mikhail,
Wan Leo C. K.,
Braun Virginie,
Heo Won Do,
Meyer Tobias,
Pelletier Laurence,
Copeland John,
Brumell John H.
Publication year - 2013
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 - 10.1111/cmi.12173
Subject(s) - formins , biology , actin , microbiology and biotechnology , salmonella , effector , cell , actin cytoskeleton , cytoskeleton , bacteria , biochemistry , genetics
Summary S almonella invade host cells using T ype 3 secreted effectors, which modulate host cellular targets to promote actin rearrangements at the cell surface that drive bacterial uptake. The Arp 2/3 complex contributes to S almonella invasion but is not essential, indicating other actin regulatory factors are involved. Here, we show a novel role for FHOD 1, a formin family member, in S almonella invasion. FHOD 1 and Arp 2/3 occupy distinct microdomains at the invasion site and control distinct aspects of membrane protrusion formation. FHOD 1 is phosphorylated during infection and this modification is required for promoting bacterial uptake by host cells. ROCK II , but not ROCK I , is recruited to the invasion site and is required for FHOD 1 phosphorylation and for S almonella invasion. Together, our studies revealan important phospho‐dependent FHOD 1 actin polymerization pathway in S almonella invasion.