SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to Signaling Complexes.

Recruitment of the deubiquitinase CYLD to signaling complexes is mediated by its interaction with HOIP, the catalytically active component of the linear ubiquitin chain assembly complex (LUBAC). Here, we identify as a constitutive direct binding partner of HOIP that bridges the interaction between CYLD and HOIP. duanyu1842TA2 recruitment to TNFR1- and NOD2-signaling complexes is dependent on HOIP, and loss of duanyu1842TA2 abolishes CYLD recruitment. Deficiency in duanyu1842TA2 exerts limited effects on gene activation pathways but diminishes necroptosis induced by tumor necrosis factor (TNF), resembling loss of CYLD. In summary, we describe duanyu1842TA2 as a previously unrecognized factor in LUBAC-dependent signaling pathways that serves as an adaptor between HOIP and CYLD, thereby enabling recruitment of CYLD to signaling complexes.

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