The linear ubiquitin (Ub) chain assembly complex (LUBAC) is an E3 ligase that specifically assembles Met1-linked (also known as linear) Ub chains that regulate nuclear factor kappaB (NFkappaB) signaling. Deubiquitinases are key regulators of Ub signaling. OTULIN (also known as FAM105B) is an OTU domain deubiquitinase with high activity and unique specificity for Met1-linked polyUb (Keusekotten K et al. 2013; Rivkin E et al. 2013). OTULIN antagonizes processes involving LUBAC, including tumor necrosis factor alpha (TNFalpha), poly(I:C), NOD2 and Wnt signaling (Fiil BK et al. 2013; Keusekotten K et al. 2013; Rivkin E et al. 2013). OTULIN interacts directly with the N-terminal PUB domain of HOIP, a component of the LUBAC complex, via a conserved PUB-interacting motif (PIM) in OTULIN (Elliott PR et al. 2014; Schaeffer V et al. 2014). Furthermore, OTULIN phosphorylation within PIM was found to prevent the LUBAC:OTULIN complex formation (Elliott PR et al. 2014).
Keusekotten, K, Elliott, PR, Glockner, L, Fiil, BK, Damgaard, RB, Kulathu, Y, Wauer, T, Hospenthal, MK, Gyrd-Hansen, M, Krappmann, D, Hofmann, K, Komander, D
Schaeffer, V, Akutsu, M, Olma, MH, Gomes, LC, Kawasaki, M, Dikic, I
Elliott, PR, Nielsen, SV, Marco-Casanova, P, Fiil, BK, Keusekotten, K, Mailand, N, Freund, SM, Gyrd-Hansen, M, Komander, D
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