Biology:SUMO2

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Small ubiquitin-related modifier 2 is a protein that in humans is encoded by the SUMO2 gene.[1]

Function

This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It is a ubiquitin-like protein and functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin, which is primarily associated with targeting proteins for proteasomal degradation, SUMO2 is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last two amino acids of the carboxy-terminus have been cleaved off. Numerous pseudogenes have been reported for this gene. Alternate transcriptional splice variants encoding different isoforms have been characterized.[2]

Interactions

SUMO2 has been shown to interact with TRIM63[3] and CFAP298.[4]


Clinical significance

Deep hypothermia protects the brain from ischemic injury, which is why it's employed for major cardiovascular procedures that necessitate cardiopulmonary bypass and a period of circulatory arrest. With an experiment [5]conducted to moderate hypothermia, small ubiquitin-like modifier (SUMO1-3) conjugation was significantly activated in the brain. The effects of hypothermia on SUMO conjugation were evaluated in this experiment[5] using Western blot and immunohistochemistry in animals that were either normothermic (37°C) or deep to moderate (18°C, 24°C, 30°C) hypothermic cardiopulmonary bypass. In these cells, even 30°C hypothermia was enough to significantly boost SUMO2/3-conjugated protein levels and nucleus accumulation. Deep hypothermia caused the SUMO-conjugating enzyme Ubc9 to translocate to the nucleus, implying that the increase in nuclear levels of SUMO2/3-conjugated proteins seen in hypothermic animals' brains is an active process. Deep hypothermia caused only a small increase in the amounts of SUMO2/3-conjugated proteins in primary neuronal cells. This shows that neurons in vivo have a greater capacity to activate this endogenous possibly neuroprotective mechanism when exposed to hypothermia than neurons in vitro. Identifying proteins that are SUMO2/3 conjugated during hypothermia could aid in the development of new preventive and therapeutic therapies to make neurons more resistant to a transient blood supply interruption.


References

  1. ↑ "Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene". Biochemical and Biophysical Research Communications 222 (1): 178–80. May 1996. doi:10.1006/bbrc.1996.0717. PMID 8630065. https://zenodo.org/record/1229472. 
  2. ↑ "Entrez Gene: SUMO2 SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6613. 
  3. ↑ "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain". The Journal of Biological Chemistry 276 (26): 23992–9. Jun 2001. doi:10.1074/jbc.M011208200. PMID 11283016. 
  4. ↑ "System-wide changes to SUMO modifications in response to heat shock". Science Signaling 2 (72): ra24. 2009. doi:10.1126/scisignal.2000282. PMID 19471022. 
  5. ↑ 5.0 5.1 Wang, Liangli; Ma, Qing; Yang, Wei; Mackensen, G. Burkhard; Paschen, Wulf (November 2012). "Moderate hypothermia induces marked increase in levels and nuclear accumulation of SUMO2/3-conjugated proteins in neurons" (in en). Journal of Neurochemistry 123 (3): 349–359. doi:10.1111/j.1471-4159.2012.07916.x. PMID 22891650. 

Further reading





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