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SPOP inhibits hepatocellular carcinoma (HCC (show FAM126A Proteins)) cell metastasis via ubiquitin-dependent SUMO1/SENP7 (show SENP7 Proteins) proteolysis and may thus serve as a new opinion for the prevention of HCC (show FAM126A Proteins) metastasis.
Study found a significant difference in the expression of Cx43 (show GJA1 Proteins) and SUMO1 between cancer stem cells and non-cancer stem cells in liver cancer. By the co-expression of Cx43 (show GJA1 Proteins) and SUMO1 in cancer stem cells, the gap junction intercellular communication of liver cancer stem cells was obviously improved.
Two SUMO modification sites existed in dopamine receptor D1 (show DRD1 Proteins), the phosphorylation of which, due to SUMO modification, can interact with PP2A (show PPP2R4 Proteins), leading to the inhibition of D1 de-phosphorylation and normal function.
The SUMO1/UBC9 (show UBE2I Proteins) axis may regulate Nox1mediated diabetic retinopathy by inhibiting reactive oxygen species generation and apoptosis.
These results suggest that SUMO1 contributes to hepatocellular carcinoma progression by promoting p65 (show GORASP1 Proteins) nuclear translocation
In summary, our study revealed a negative regulation of the UPR transducer ATF6 (show ATF6 Proteins) through post-translational SUMOylation. The information from this study will not only increase our understanding of the fine-tuning regulation of the UPR signaling but will also be informative to the modulation of the UPR for therapeutic benefits.
Molecular dynamics simulations showed that binding of the beta-grasp domain of SUMO1 induces significant conformational and dynamic changes in SENP1 (show SENP1 Proteins), including widening of the exosite cleft and quenching of nanosecond dynamics in all but a distal region.
Mutational analysis of functional sites showed that both peroxidase and PLA2 (show YWHAZ Proteins) active sites were necessary for mutant Prdx6 (show PRDX6 Proteins) function, and that Prdx6 (show PRDX6 Proteins) phosphorylation (at T177 residue) was essential for optimum PLA2 (show YWHAZ Proteins) activity.Mutant Prdx6 (show PRDX6 Proteins) at its Sumo1 sites escapes and abates this adverse process by maintaining its integrity and gaining function
SUMO and p21Cip1 (show CDKN1A Proteins) regulate the transit of proteins through the nucleolus; disruption of nucleolar export by DNA damage induces SUMO and p21Cip1 (show CDKN1A Proteins) to act as hub proteins to form a multiprotein complex in the nucleolus.
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.
SUMO chain formation relies on the amino-terminal region of SCE1 and has dedicated substrates in plants.
Functionally similar to human SUMO2 and SUMO3, Arabidopsis SUMO1 and 2 can form chains, even though they do not possess a consensus SUMOylation motif. The surprising finding that plants have dedicated enzymes for chain synthesis implies a specific role for SUMO chains in plants
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.
SUMO1 becomes conjugated with ubiquitin during heat stress, showing posttranslational modifications.
SUM3 (show SUMO3 Proteins) promotes plant defense downstream of salicylic acid, while SUM1 and SUM2 (show SUMO2 Proteins) together prevent salicylic acid accumulation in noninfected plants.
SIZ1-mediated conjugation of SUMO1 and SUMO2 (show SUMO2 Proteins) to other intracellular proteins is essential in Arabidopsis, possibly through stress-induced modification of a potentially diverse pool of nuclear proteins.
results support the critical role of SUMO-1 in SERCA2a (show ATP2A2 Proteins) function and underline the therapeutic potential of SUMO-1 for HF patients
Analysis of protein interactions showed that K179A, K180A, and K221A substitutions of classical swine fever virus core protein disrupt core-SUMO-1 binding, while K220A substitution precludes core-UBC9 (show UBE2I Proteins) binding.
The gene knockout technique is important in xenotransplantation research; here we have described the molecular cloning of SUMO-1 gene that may be a candidates to overcome the poor rate of homologous recombination.
integrity is required for PLK1 localization with SUMO-1 but not with SUMO-2 (show SUMO2 Proteins)/3. Inhibition of SUMOylation disrupts proper meiotic bipolar spindle organization and spindle-kinetochore attachment.
These findings indicate that SUMO1-conjugation of synaptic proteins does not occur or is extremely rare and hence not detectable using current methodology.
Study found expression of several mutated forms of SOD1 (show SOD1 Proteins) in the NSC-34 motor neuronal cells induces the formation of cytosolic and sometimes nuclear aggregates containing the SUMO-1 protein and showed that the formation of these aggregates can be modulated by action on the K75 (show KRT75 Proteins) SUMOylation site
The LKB1 (show STK11 Proteins) K178R SUMO mutant had defective AMPK (show PRKAA1 Proteins) signaling and mitochondrial function, inducing death in energy-deprived cells.
These findings point to a significant contribution of SUMO1 modification on neuronal function which may have implications for mechanisms involved in mental retardation and neurodegeneration.
PML (show PML Proteins) IV/ARF interaction enhances p53 (show TP53 Proteins) SUMO-1 conjugation, activation, and senescence.
SUMO1 accelerates the accumulation of autophagic vacuoles and promotes Abeta (show APP Proteins) production.
The present study used immunohistochemical and immunoblot analysis with the different developmental stages of mice and demonstrated the developmentally regulated distribution of SUMO1.
The results of this study indicate that post-translational modifications of SERCA2a (show ATP2A2 Proteins) caused by the toxic environment of the hypertrophied and failing myocardium can be prevented by SUMO-1.
SUMO-1 plays crucial roles for spindle organization, chromosome congression, and chromosome segregation during mouse oocyte meiotic maturation.
This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It 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 targets proteins for degradation, this protein 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 four amino acids of the carboxy-terminus have been cleaved off. Several pseudogenes have been reported for this gene. Alternate transcriptional splice variants encoding different isoforms have been characterized.
SMT3 suppressor of mif two 3 homolog 1
, small ubiquitin-related modifier 1
, small ubiquitin-related modifier-1
, ubiquitin-like 1 (sentrin)
, GAP modifying protein 1
, SMT3 homolog 3
, ubiquitin-homology domain protein PIC1
, ubiquitin-like protein SMT3C
, ubiquitin-like protein UBL1
, SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae)
, SMT3 suppressor of mif two 3-like 1
, small ubiquitin-related modifier 1-B
, small ubiquitin-related protein 1
, smt3 suppressor of mif two 3 homolog 1
, SUMO-1 related peptidase
, ubiquitin-like 1
, small ubiquitin-like modifier 1