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Sci Rep ; 5: 18479, 2015 Dec 21.
Article in English | MEDLINE | ID: mdl-26686473

ABSTRACT

Inflammasomes are multiprotein complexes that include members of the NOD-like receptor family and caspase-1. Caspase-1 is required for the fusion of the Legionella vacuole with lysosomes. Caspase-11, independently of the inflammasome, also promotes phagolysosomal fusion. However, it is unclear how these proteases alter intracellular trafficking. Here, we show that caspase-11 and caspase-1 function in opposing manners to phosphorylate and dephosphorylate cofilin, respectively upon infection with Legionella. Caspase-11 targets cofilin via the RhoA GTPase, whereas caspase-1 engages the Slingshot phosphatase. The absence of either caspase-11 or caspase-1 maintains actin in the polymerized or depolymerized form, respectively and averts the fusion of pathogen-containing vacuoles with lysosomes. Therefore, caspase-11 and caspase-1 converge on the actin machinery with opposing effects to promote vesicular trafficking.


Subject(s)
Actins/metabolism , Caspase 1/genetics , Cofilin 1/genetics , Legionnaires' Disease/genetics , Phosphoprotein Phosphatases/metabolism , rhoA GTP-Binding Protein/metabolism , Actins/genetics , Animals , Caspase 1/metabolism , Cofilin 1/metabolism , Humans , Inflammasomes/genetics , Inflammasomes/metabolism , Legionella pneumophila/genetics , Legionella pneumophila/pathogenicity , Legionnaires' Disease/metabolism , Legionnaires' Disease/pathology , Lysosomes/genetics , Lysosomes/metabolism , Mice , Mice, Knockout , Multiprotein Complexes/genetics , Multiprotein Complexes/metabolism , Phosphoprotein Phosphatases/genetics , Receptors, Cell Surface/genetics , Receptors, Cell Surface/metabolism , Vacuoles/genetics , Vacuoles/metabolism , Vesicular Transport Proteins/genetics , Vesicular Transport Proteins/metabolism , rhoA GTP-Binding Protein/genetics
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