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Linear ubiquitin chain‐binding domains
Author(s) -
Fennell Lilian M.,
Rahighi Simin,
Ikeda Fumiyo
Publication year - 2018
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14478
Subject(s) - ubiquitin , microbiology and biotechnology , ubiquitin protein ligases , ubiquitin conjugating enzyme , deubiquitinating enzyme , ubiquitin ligase , plasma protein binding , chemistry , biology , computational biology , biochemistry , gene
Ubiquitin modification (ubiquitination) of target proteins can vary with respect to chain lengths, linkage type, and chain forms, such as homologous, mixed, and branched ubiquitin chains. Thus, ubiquitination can generate multiple unique surfaces on a target protein substrate. Ubiquitin‐binding domains ( UBD s) recognize ubiquitinated substrates, by specifically binding to these unique surfaces, modulate the formation of cellular signaling complexes and regulate downstream signaling cascades. Among the eight different homotypic chain types, Met1‐linked (also termed linear) chains are the only chains in which linkage occurs on a non‐Lys residue of ubiquitin. Linear ubiquitin chains have been implicated in immune responses, cell death and autophagy, and several UBD s ‐ specific for linear ubiquitin chains ‐ have been identified. In this review, we describe the main principles of ubiquitin recognition by UBD s, focusing on linear ubiquitin chains and their roles in biology.