Sumoylation

The covalent attachment of a small ubiquitin-related modifier (SUMO) to substrate protein, a process that is biochemically analogous to, but functionally distinct from, ubiquitination; sumoylation is critical to many different biological processes—e.g., protein localisation and stability, transcriptional activities, nucleocytoplasmic signalling and transport, genome replication, and regulation of gene expression
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Although the most common mechanism involved in epigenetics (or perhaps the one most often heard about) is that of methylation, other pretranscriptional and post-translational mechanisms include histone modification (through de/acetylation), ubiquitination, sumoylation, and RNA- and polycomb-based functions, although these are not fully understood.
However, NINDS senior investigator John Hallenbeck, co-senior author of the study found that a cellular process called SUMOylation goes into overdrive in a certain species of ground squirrel during hibernation.
LaminB1 also undergoes some forms of post-translational modifications, such as farnesylation [29], phosphorylation, glycosylation, and sumoylation [30], which are linked to the significant conformational changes of their target proteins [31].
However, despite these links with human health and ageing, and the identification of many SUMOylated substrates, there is much to learn about how SUMOylation influences human health.
Then, HIF-1[alpha] is accumulated in the cytoplasm under hypoxic condition rapidl and modified by sumoylation, s-nitrosylation, acetylation and phosphorylation (24).
Indeed, while acetylation and methylation are the most studied phenomena, histones are also submitted to phosphorylation, sumoylation, ubiquitination, and ribosylation.
Activating transcription factor 3 SUMOylation is involved in angiotensin II-induced endothelial cell inflammation and dysfunction.
The different type of histone modifications include methylation, phosphorylation, acetylation, sumoylation and ubiqutination of histones residues.
Additionally, their activity is subject to regulation by posttranslational modifications, such as phosphorylation, SUMOylation, and ubiquitination (5).
Zhou et al., "High glucose induces activation of NF-[kappa]B inflammatory signaling through I[kappa]B[alpha] sumoylation in rat mesangial cells," Biochemical and Biophysical Research Communications, vol.