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Selectivity of the ubiquitin‐binding modules
Author(s) -
Rahighi Simin,
Dikic Ivan
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.04.053
Subject(s) - ubiquitin , deubiquitinating enzyme , ubiquitin conjugating enzyme , ubiquitin ligase , microbiology and biotechnology , chemistry , biochemistry , endocytosis , ubiquitin protein ligases , transcription factor , biology , receptor , gene
Ubiquitin‐binding modules are constituents of cellular proteins that mediate the effects of ubiquitylation by making transient, non‐covalent interactions with ubiquitin molecules. While some ubiquitin‐binding modules bind single ubiquitin moieties, others are selective for specific ubiquitin chains of different linkage types and lengths. In recent years, functions of ubiquitin chains that are polymerized through their Lys or N‐terminal Met (i.e. linear chains) residues have been linked to a variety of cellular processes. Selectivity of ubiquitin‐binding modules for different ubiquitin chain types appears as a key to the distinct regulatory consequences during protein quality control pathways, receptor endocytosis, gene transcription, signaling via the NF‐κB pathway, and autophagy.