SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?
By G. Gill. Genes & Development, 2004
800 citations recorded by the source corpus.
The small ubiquitin-related modifier SUMO posttranslationally modifies many proteins with roles in diverse processes including regulation of transcription, chromatin structure, and DNA repair. Similar to nonproteolytic roles of ubiquitin, SUMO modification regulates protein localization and activity. Some proteins can be modified by SUMO and ubiquitin, but with distinct functional consequences. It is possible that the effects of ubiquitination and SUMOylation are both largely due to binding of proteins bearing specific interaction domains. Both modifications are reversible, and in some cases dynamic cycles of modification may be required for activity. Studies of SUMO and ubiquitin in the nucleus are yielding new insights into regulation of gene expression, genome maintenance, and signal transduction.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/3c7f0ba393024605d31f65aa325653aeab49072e
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In Molecular Biology
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- Arvind Kumar
- Nadia M. Tsankova
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- G. Koob
- Colleen A. Mcclung
- Nora D. Volkow
In Oncology
Citations in the corpus
- Epigenetic regulation in psychiatric disorders (2007, background): “The roles of histone ubiquitylation, SUMOylation and ADP ribosylation are less well understoo”
- Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins (2007, background): “SUMOylation and de-SUMOylation are known to be critical in regulating the partitioning of proteins between nucleus and cytoplasm (Gill, 2004; Johnson, 2004), and in Dictyostelium MEK1 is subject”
- Ubiquitin and ubiquitin-like proteins as multifunctional signals (2005, background): “Defects in and the manipulation of sumoylation have been implicated in several unrelated disease”