| Background | Ubiquitination, onetypeofthemostcommonpost-translationalmodification, mediatestheregulationofproteinhomeostasisinvivo. Substrate proteins can be modified with single ubiquitin moieties or with polymeric ubiquitin chains. Within polyubiquitin chains, ubiquitin can form eight different linkage types, using one of seven internal lysine residues (K6, K11, K27, K29, K33, K48, K63) or methionine at position 1 (M1).Here we focus on a distinct type of ubiquitination that is characterized by an inter-ubiquitin linkage through the N-terminal methionine, called M1-linked or linear ubiquitination. Formation, recognition, and disassembly of linear ubiquitin chains are highly specific processes that are implicated in immune signaling, cell death regulation and protein quality control. Consistent with their role in influencing signaling events, linear ubiquitin chains are formed in a transient and spatially regulated manner, making their detection and quantification challenging. |
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