Disease relevance of SUMO3

• In addition, SUMO-3 immunoreactivity is predominantly detected in neurons in brains from AD, Down's syndrome, and nondemented humans [1].
• Through a yeast functional screen, we have identified SUMO-3 as a regulator of androgen receptor activity in prostate cancer cells [2].
• Down-regulation of SMT3A gene expression in association with DNA synthesis induction after X-ray irradiation in nevoid basal cell carcinoma syndrome (NBCCS) cells [3].

High impact information on SUMO3

• Increased protein sumoylation resulting from overexpression of SUMO-3 dramatically reduces Abeta production [1].
• Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3 [4].
• SENP5 showed SUMO-3 C-terminal hydrolase activity but could not process pro-SUMO-1 in vitro [4].
• In contrast, SUMO-3 and it close relative SUMO-2 strongly enhance transactivation by endogenous androgen receptor in LNCaP cells [2].
• SUMO-3 enhances androgen receptor transcriptional activity through a sumoylation-independent mechanism in prostate cancer cells [2].

Biological context of SUMO3

• Human SMT3A cDNA was identified from the genome sequencing project of chromosome 21 (5) [5].
• Another genomic DNA fragment of 1,531 nucleotides, containing 7% differences from that of cDNA, is unable to encode a functional protein, and thus, it is a SMT3A processed pseudogene [5].
• The nucleotide sequence of a PCR-amplified SMT3A genomic DNA fragment was found to be identical to that of SMT3A cDNA, indicating the absence of intron(s) in its protein coding region [5].
• SUMO-2 and SUMO-3 localized to chromosome earlier and accumulated gradually during telophase [6].
• The protein-coding sequence of the SUMO-1 gene is interrupted by four introns, while those of SUMO-2 and SUMO-3 genes are interrupted by three introns [7].

Anatomical context of SUMO3

• In primary prostate epithelial cells, PrEC, and the prostate cancer cells, PC-3, SUMO-3 has a weak negative effect on androgen receptor transcriptional activity [2].
• In addition to NBCCS cells, normal fibroblast cells showed the DNA synthesis induction after X-ray irradiation when they were treated with antisense oligonucleotides (AO) for SMT3A [3].

Associations of SUMO3 with chemical compounds

• Stable overexpression of SUMO-3 in LNCaP cells significantly enhances the androgen-dependent proliferation of these cells [2].

Physical interactions of SUMO3

• Solution structure of human SUMO-3 C47S and its binding surface for Ubc9 [8].
• We used NMR spectroscopy to solve the solution structure of the SIM of MCAF1 bound to SUMO-3 [9].

Other interactions of SUMO3

• A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3 [10].
• Notably, the negatively charged surface of SUMO-3 C47S is highly complementary in its electrostatic potentials and hydrophobicity to the positively charged surface of Ubc9 [8].
• Moreover, we demonstrate that oligomerization of SUMO-3 is required for PML retention in the nucleus [11].
• Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase [12].
• A novel cDNA, termed SMT3A, was isolated and mapped between the loci PFKL and D21S171, about 2.2 Mb proximal to the telomere [13].

References