LUBAC binds OTULIN

Stable Identifier
R-HSA-5661517
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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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 kappa-B (NF-kappa-B) signaling. Deubiquitinases are key regulators of Ub signaling. OTULIN (also known as FAM105B) is an OTU domain deubiquitinase which specifically disassembles Met1-linked polyUb generated by LUBAC (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 at Tyr56 within PIM was found to prevent the LUBAC:OTULIN complex formation (Elliott PR et al. 2014).

Literature References
PubMed ID Title Journal Year
24726327 Binding of OTULIN to the PUB domain of HOIP controls NF-?B signaling

Olma, MH, Kawasaki, M, Gomes, LC, Dikic, I, Schaeffer, V, Akutsu, M

Mol. Cell 2014
23746843 OTULIN antagonizes LUBAC signaling by specifically hydrolyzing Met1-linked polyubiquitin

Krappmann, D, Hospenthal, MK, Kulathu, Y, Keusekotten, K, Damgaard, RB, Hofmann, K, Glockner, L, Elliott, PR, Wauer, T, Fiil, BK, Komander, D, Gyrd-Hansen, M

Cell 2013
24726323 Molecular basis and regulation of OTULIN-LUBAC interaction

Elliott, PR, Keusekotten, K, Freund, SM, Nielsen, SV, Marco-Casanova, P, Fiil, BK, Komander, D, Mailand, N, Gyrd-Hansen, M

Mol. Cell 2014
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