Ubiquitylation and cell signaling

By K. Haglund, Ivan Dikic. EMBO Journal, 2005

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Reading protein modifications with interaction domains (2006, background): “The phosphorylated protein is then ubiquitylated and is consequently recognized by the ubiquitin-binding domain (UBD) of a protein that regulates events such as endocytosis or proteolysi”
Targeting the ubiquitin system in cancer therapy (2009, background): “With time, however, an increasing number of distinct functions have been assigned to different types of ubiquitin modification (for example, the addition of a single ubiquitin molecule or a ubiquitin chain), such as the regulation of protein trafficking, the assembly of protein signalling complexes,”
Ubiquitination and selective autophagy (2012, background): “or single ubiquitin moieties (monoubiquitination) were thought to signal mainly for non-proteolytical functions.(14,15) These chain types are involved in controlling several processes such as receptor transport, DNA repair and signalling.”
Modification of proteins by ubiquitin and ubiquitin-like proteins. (2006, background): “Ubiquitin has seven lysine residues, all of which are potentially involved in chain formation, although ubiquitin-Lys48 and -Lys63 are the best-characterized residues involved in polyubiquitylation (Haglund & Dikic 2005).”