The Ubiquitination Machinery: Its Versatile Role in Normal and Disease-Related Cellular Processes

Dear Colleagues,

Ubiquitination is a widespread and reversible post-translational modification of eukaryotic proteins, in which ubiquitin (Ub) or ubiquitin-like proteins (UbL) are conjugated to protein substrates by an enzyme cascade. The Ub and UbL marks are only transient, since deubiquitinating enzymes (DUBs) hydrolyze the covalent bonds linking these marks to substrates. The Ub and UbL functional interplay modulates protein stability, activity or localization, or protein–protein interaction, thus representing a dynamic system that vitally regulates an increasing number of cellular processes. Simultaneous ubiquitin-dependent processes compete for limited Ub and UbL pools and, thus, must be tightly coordinated by constant ubiquitination-deubiquitination cycles.

Several decades of research pinned down many components, substrates, and regulatory pathways of the highly complex ubiquitination machinery. Various disruptions of this system are implicated in the genesis of many human diseases, such as neurodegeneration, inflammation, or cancer. Therefore, a better understanding of the ubiquitination system is crucial for developing therapeutic or preventative measures against these diseases.

In this Special Issue of the International Journal of Molecular Sciences, we would like to invite contributions addressing the functional analysis of ubiquitination machinery components or identifying new substrates or regulatory circuits, with an emphasis on pathological implications or therapeutic prospects. Submissions can either be original research papers or reviews. Your contributions will be highly appreciated.

Dr. Peter Deak
Dr. Yuu Kimata
Dr. Levente Kovács
Guest Editors

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