Signaling through monoubiquitination.
Ubiquitination is a post-translational modification in which a small conserved peptide, ubiquitin, is appended to target proteins in the cell, through a series of complex enzymatic reactions. Recently, a particular form of ubiquitination, monoubiquitination, has emerged as a nonproteolytic reversible modification that controls protein function. In this review, we highlight recent findings on monoubiquitination as a signaling-induced modification, controlled, among others, by pathways originating from active receptor tyrosine kinases. Furthermore, we review the major cellular processes controlled by ubiquitin modification, including membrane trafficking, histone function, transcription regulation, DNA repair, and DNA replication.
Sigismund
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IFOM, The FIRC Institute for Molecular Oncology, Via Adamello 16, 20139 Milan, Italy.
Polo
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Di Fiore
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D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D004260:DNA Repair; D004261:DNA Replication; D004705:Endocytosis; D005199:Fanconi Anemia / Q000378:metabolism; D006801:Humans; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D050721:Proto-Oncogene Proteins c-cbl; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D015398:Signal Transduction; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism
D011518:Proto-Oncogene Proteins; D025801:Ubiquitin; D050721:Proto-Oncogene Proteins c-cbl; D044767:Ubiquitin-Protein Ligases; D020794:Receptor Protein-Tyrosine Kinases