Unknown

Dataset Information

0

Caspase-11 and caspase-1 differentially modulate actin polymerization via RhoA and Slingshot proteins to promote bacterial clearance.


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.

SUBMITTER: Caution K 

PROVIDER: S-EPMC4685268 | biostudies-other | 2015 Dec

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC3408798 | biostudies-literature
| S-EPMC4592971 | biostudies-literature
| S-EPMC1283440 | biostudies-literature
| S-EPMC5625121 | biostudies-literature
| S-EPMC6893291 | biostudies-literature
| S-EPMC5828612 | biostudies-literature
| S-EPMC2584996 | biostudies-literature
| S-EPMC7645254 | biostudies-literature
| S-EPMC4157630 | biostudies-literature
| S-EPMC8633687 | biostudies-literature