Ubiquitin proteolytic system: focus on SUMO
| Autor: | Phillip R. Heaton, Van G. Wilson |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Proteomics Proteasome Endopeptidase Complex Saccharomyces cerevisiae Proteins Ubiquitin-Protein Ligases Lysine SUMO protein Protein Array Analysis SUMO enzymes Computational biology Biology Biochemistry Mass Spectrometry Article Ligases Mice Ubiquitin Small Ubiquitin-Related Modifier Proteins Two-Hybrid System Techniques Endopeptidases Animals Humans Caenorhabditis elegans Proteins Molecular Biology Conserved Sequence Tandem affinity purification Ubiquitination Nuclear Proteins Neoplasm Proteins biology.protein Protein Processing Post-Translational |
| Zdroj: | Expert review of proteomics. 5(1) |
| ISSN: | 1744-8387 |
| Popis: | The Small Ubiquitin-like Modifier proteins (Smt3 in yeast and SUMOs 1-4 in vertebrates) are members of the ubiquitin super family. Like ubiquitin, the SUMOs are protein modifiers that are covalently attached to the epsilon amino group of lysine residues in the substrates. The application of proteomics to the SUMO field has greatly expanded both the number of known targets and the number of identified target lysines. As new refinements of proteomic techniques are developed and applied to sumoylation, an explosion of novel data is likely in the next five years. This ability to examine sumoylated proteins globally, rather than individually, will lead to new insights into both the functions of the individual SUMO types and to how dynamic changes in overall sumoylation occur in response to alterations in cellular environment. In addition, there is a growing appreciation for the existence of crosstalk mechanisms between the sumoylation and ubiquitinylation processes. Rather than being strictly parallel, these two systems have many points of intersection, and It is likely that coordination of these two systems is a critical contributor to the regulation of many fundamental cellular events. |
| Databáze: | OpenAIRE |
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