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Comment
. 2012 Dec 13;12(6):737-8.
doi: 10.1016/j.chom.2012.11.006.

YopM puts caspase-1 on ice

Ine Jørgensen  1 , Edward A Miao
Affiliations
Comment

YopM puts caspase-1 on ice

Ine Jørgensen et al. Cell Host Microbe. .

Abstract

Caspase-1-mediated detection of pathogens is a potent arm of the innate immune system. LaRock and Cookson (2012) show that the Yersinia type III secretion effector, YopM, directly inhibits caspase-1.

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Figures

Figure 1
Figure 1. YopM inhibits Caspase-1
Yersinia T3SS activity is detected by cytosolic inflammasomes by unknown mechanisms. Oligomerized NLR inflammasomes recruit the adaptor protein ASC through homotypic interactions between CARD (pink) or pyrin (purple) domains. ASC is composed of a CARD and a pyrin domain, and subsequently collects the entire complement of cellular ASC into a single focus. The ASC-CARD domains then recruit pro-Caspase-1 via it’s CARD domain, resulting in its auto-proteolytic processing and activation. YopM contains a pseudo-substrate binding site that binds and retains activated Caspase-1. Because YopM contains a nuclear localization signal, sequestration of activated Caspase-1 in the nucleus may be a key mechanism by which YopM separates Caspase-1 from it’s intended targets.
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Comment on

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