A New DUB Makes Linear Ubiquitin a Party to Its Own Destruction Reuven Wiener, Cynthia Wolberger  Cell  Volume 153, Issue 6, Pages 1189-1191 (June 2013) DOI: 10.1016/j.cell.2013.05.018 Copyright © 2013 Elsevier Inc. Terms and Conditions

Figure 1 OTULIN Acts as the DUB for Linear Ubiquitin Chains (A) The E3 ligase complex LUBAC assembles linear Ub by forming peptide bonds between the N and C termini of successive Ub monomers. These peptide bonds are cleaved by OTULIN, which disassembles linear polyUb chains and releases monomeric Ub. (B) OTULIN binds to diUb, positioning the peptide bond that joins Met1 of the proximal Ub with the C-terminal Gly76 of the distal Ub in the OTULIN active site. Glu16 (E16) of the proximal Ub inserts into the active site and helps to position the catalytic triad for catalysis. (C) OTULIN antagonizes LUBAC signaling. Linear Ub chains are involved in TNFα signaling, downstream activation of MAPK, and the translocation of NF-κB to the nucleus. Cell 2013 153, 1189-1191DOI: (10.1016/j.cell.2013.05.018) Copyright © 2013 Elsevier Inc. Terms and Conditions