A cell-free system combined with cell-based assays elucidate the biochemical mechanism of signal transduction mediated by the mitochondrial protein MAVS and delineates the role of ubiquitin E3 ligases in antiviral innate immune responses.

Skin inflammation in Sharpin-deficient mice is primarily due to TNFR1-dependent apoptosis, but necroptosis appears to play a bigger role in inflammation of internal organs.

The adaptor proteins FADD and TRADD play an important role in the Sharpin-dependent anti-apoptosis signaling pathway in keratinocytes and regulate skin homeostasis.

HOIL-1 deficiency in mice results in a severe immunodeficiency that is effectively complemented by chronic infection with a murine gamma-herpesvirus.

The E3 ubiquitin ligase complex linear ubiquitin chain assembly complex (LUBAC) forms a branched chain on linear ubiquitin chains depending on the RING-in-between-RING-type E3 ligase heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1L).

Biochemical and structural analyses reveal direct ubiquitin modification of single-stranded nucleic acids, catalysed by the DTX3L ubiquitin ligase.