Figure 1.

Schematic representation of the LUBAC components, SHARPIN, HOIP and HOIL-1. There is significant sequence homology (45% identity) between the carboxyl terminus of SHARPIN and the amino terminus of HOIL-1, each of which contains a UBL and an NZF motif. HOIP is the catalytic subunit of the tripartite LUBAC with SHARPIN and HOIL-1 as accessory factors that bind via their respective UBL domains to the NZF2 and UBA domains of HOIP, respectively. HOIP, SHARPIN and HOIL-1 also bind to ubiquitin chains through NZF-mediated interactions. The functions of the ZnF domain of HOIP and the coiled-coil domain of SHARPIN are currently unknown. The RBR domain of HOIP, but not of HOIL-1, is responsible for linear ubiquitin chain generation by LUBAC. Arrows indicate confirmed interactions between the proteins. Abbreviations: ZnF, zinc finger; NZF, Npl4 zinc finger; UBL, ubiquitin-like domain; UBA, ubiquitin-associated domain; IBR, in-between RING domain; RBR, RING-IBR-RING domain.

Walczak et al. BMC Biology 2012 10:23   doi:10.1186/1741-7007-10-23
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