Ubiquitin and Ubiquitin-Like Pathways in Development and Disease

Dear Colleagues,

Originally discovered as a tag for protein destruction, modification of proteins by ubiquitin (Ub) has numerous physiological roles beyond protein degradation, regulating almost every aspect of the cell’s activities. In recent years, our understanding of the biology of the Ub pathway has greatly expended; it includes in-depth understanding of the extensive enzymatic machinery that catalyzes ubiquitination, function-specific types of poly-ubiquitin chains, the regulation of enzymes within the pathway, and the activity of the protein-degrading nanomachine, the proteasome. The importance of reversing ubiquitination by iso-peptidases (DUBs) has also gained much attention. Moreover, in the last three decades, post-translational modifications by ubiquitin-like (UbL) proteins were discovered. UbLs also regulate diverse and essential cellular processes. The discovery of direct enzymatic crosstalk between Ub and UbL pathways unveiled an important layer of cellular regulation. These discoveries were possible, in part, by the development of unbiased Ub/UbL-specific proteomic tools. The aim of this Special Issue is to share recent advances regarding the biology of ubiquitin and ubiquitin-like pathways in development using model organisms and humans. Among the topics are the biology of ubiquitin ligases, iso-peptidases, the proteasome, signalosome, and ubiquitin-like proteins, such as SUMO, and ISG15. A specific emphasis is given to the intimate link between Ub/UbL pathways and diseases such as cancer and neurodegeneration, portraying the heterogenous landscape of Ub/UbL pathways in current biology.

Prof. Amir Orian
Guest Editor

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