Author:

Keywords:

Science & Technology, Life Sciences & Biomedicine, Physical Sciences, Biochemistry & Molecular Biology, Chemistry, Multidisciplinary, Chemistry, ubiquitin system, genetic diseases, ubiquitin ligase, deubiquitinases, monoubiquitin signaling, vesicular trafficking, protein complex formation, E3 UBIQUITIN LIGASE, C-CBL INHIBITION, FANCONI-ANEMIA, DEUBIQUITINATING ENZYME, H2B UBIQUITYLATION, BINDING DOMAINS, LRSAM1 MUTATION, PROTEIN LIGASE, USP8 MUTATIONS, EGF RECEPTOR, Deubiquitinating Enzymes, Genetic Diseases, Inborn, Humans, Proteasome Endopeptidase Complex, Protein Binding, Protein Interaction Mapping, Protein Processing, Post-Translational, Protein Stability, Protein Transport, Proteolysis, Subcellular Fractions, Substrate Specificity, Ubiquitin, Ubiquitin-Protein Ligase Complexes, Ubiquitinated Proteins, Ubiquitination, 0399 Other Chemical Sciences, 0604 Genetics, 0699 Other Biological Sciences, Chemical Physics, 3101 Biochemistry and cell biology, 3107 Microbiology, 3404 Medicinal and biomolecular chemistry

Abstract:

Ubiquitination is a versatile and dynamic post-translational modification in which single ubiquitin molecules or polyubiquitin chains are attached to target proteins, giving rise to mono- or poly-ubiquitination, respectively. The majority of research in the ubiquitin field focused on degradative polyubiquitination, whereas more recent studies uncovered the role of single ubiquitin modification in important physiological processes. Monoubiquitination can modulate the stability, subcellular localization, binding properties, and activity of the target proteins. Understanding the function of monoubiquitination in normal physiology and pathology has important therapeutic implications, as alterations in the monoubiquitin pathway are found in a broad range of genetic diseases. This review highlights a link between monoubiquitin signaling and the pathogenesis of genetic disorders.