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Increased post-translational modification of proteins by SUMO-2/3 is a cytoprotective response against cell stress induced by ischaemia and reperfusion.
Sumoylation of PML (show PML Proteins) with SUMO2 by UBC9/UBE2I (show UBE2I Proteins) can lead to formation of polymeric SUMO chains. Data suggest that coordination of growing poly-SUMO chain with "back side" binding site on UBC9/UBE2I (show UBE2I Proteins) appears to be required for SUMO chain elongation on PML (show PML Proteins). (PML (show PML Proteins) = promyelocytic leukemia protein (show PML Proteins); SUMO2 = small ubiquitin-like modifier 2; UBC9/UBE2I (show UBE2I Proteins) = ubiquitin-conjugating enzyme (show Ube2t Proteins) UBC9/UBE2I (show UBE2I Proteins))
The data demonstrate that SUMO2 conjugation and SENP3 (show ULP1 Proteins)-driven deSUMOylation of PELP1 (show PELP1 Proteins) is instrumental for ordered progression of ribosome maturation, and they provide molecular insight into the dynamics of ribosome maturation.
Data suggest that PIASy (show PIAS4 Proteins) exhibits a SIM (show SIM2 Proteins) (SUMO-interacting motif) in addition to the SIM (show SIM2 Proteins) identified in homologous proteins in other species; both SIMs are located near C terminus of PIASy (show PIAS4 Proteins), and both are required for full ligase activity of PIASy (show PIAS4 Proteins); hydrophobic core residues of the new SIM (show SIM2 Proteins) are essential in binding to SUMO-3 (show SUMO3 Proteins). (PIASy (show PIAS4 Proteins) = protein inhibitors of activated STAT (show STAT1 Proteins) y; SUMO-3 (show SUMO3 Proteins) = small ubiquitin-like modifier 3 (show SUMO3 Proteins))
This study reveals an essential role of SUMOylated FADD (show FADD Proteins) in Drp1 (show CRMP1 Proteins)- and caspase-10 (show CASP10 Proteins)-dependent necrosis.
The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation.
This study demonstrated that two polymorphisms of SUMO2 were significantly associated with an increased risk of AD in female group.
FOXP2 (show FOXP2 Proteins) can be modified with all three human SUMO proteins and that PIAS1 (show PIAS1 Proteins) promotes this process.
Hsp27-Ubc9 pathway recognizes the conformation of mutant CFTR which leads to its SUMO-2 conjugation and degradation by the ubiquitin-proteasome system.
Data suggest that RAP80 (show UIMC1 Proteins) SIM (show SIM2 Proteins) (SUMO interacting motif) binds SUMO-2; both specificity and affinity are enhanced through phosphorylation of canonical CK2 (show CSNK2A1 Proteins) (casein kinase 2) site within the SIM (show SIM2 Proteins).
cyclin E (show CCNE1 Proteins) is dynamically and highly conjugated to SUMO2/3 on chromatin, independently of Cdk2 (show CDK2 Proteins) activity and origin activation.
we provide evidence for the existence of a preferential conjugation of AtSUMO1/2 compared with AtSUMO3/5, which is determined by a role of the E1-activating enzyme in SUMO paralogue discrimination.
SUM3 (show SUMO3 Proteins) promotes plant defense downstream of salicylic acid, while SUM1 (show SUMO1 Proteins) and SUM2 together prevent salicylic acid accumulation in noninfected plants.
SIZ1-mediated conjugation of SUMO1 (show SUMO1 Proteins) and SUMO2 to other intracellular proteins is essential in Arabidopsis, possibly through stress-induced modification of a potentially diverse pool of nuclear proteins.
SUMO-2 inhibits aggregation of CPEB3 (show CPEB3 Proteins).
The present study used immunohistochemical and immunoblot analysis with the different developmental stages of mice and demonstrated the developmentally regulated distribution of SUMO2/3 in the brain.
SUMO-2-Tg mouse lines exhibited cardiomyopathy with various severities. SUMO-2 directly regulated apoptosis by at least partially targeting calpain 2 (show CAPN2 Proteins) and calpastatin (show CAST Proteins).
Results indicate that a functional SUMO1 (show SUMO1 Proteins)-3 expression is essential for emotionality and cognition
Expression levels and not functional differences between SUMO2 and SUMO3 (show SUMO3 Proteins) are critical for normal embryogenesis.
Stress-induced phosphorylation of Thr486 in c-Myb (show MYB Proteins) by p38 (show CRK Proteins) mitogen-activated protein kinases attenuates conjugation of SUMO-2/3.
post-ischemic activation of SUMO2/3 conjugation may define the fate of neurons exposed to a transient interruption of blood supply
Alterations in SUMO substrate conjugation may occur and global posttranslational modifications by ubiquitin may play an important role in the mechanisms underlying Alzheimer disease.
activation of SUMO2/3 conjugation is an endogenous neuroprotective stress response.
These results indicate that the functional role of SUMO-2/3 in the regulation of NFkappaB activity was conserved during evolution.
SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002
SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)
, small ubiquitin-related modifier 2
, SMT3 homolog 2
, SMT3 suppressor of mif two 3 homolog 2
, sentrin 2
, ubiquitin-like protein SMT3A
, ubiquitin-like protein SMT3B
, small ubiquitin-related modifier 2-B
, SMT3 homolog 1
, SMT3 suppressor of mif two 3 homolog 1
, SMT3 suppressor of mif two 3 homolog 3
, small ubiquitin-related modifier 3
, MIF2 suppressor
, SMT3 supressor of mif two 3 homolog 2