Abstract
The human paracaspase MALT1 is a caspase homolog that plays a central role in NF-κB signaling. Over the past few years it has become clear that this is due to a combination of its scaffolding and proteolytic function. Knockout mice and mice expressing a catalytically dead variant of the protease have provided valuable information. This review aims to provide an overview of recent developments regarding the enzymatic mechanism and specificity of MALT1, its substrates discovered to date, different mouse models, as well as the role of MALT1 in NF-κB signaling downstream of a variety of different receptors.