SUMOylation of damaged DNA-binding protein DDB2

Tsuge, Maasa; Masuda, Yusuke; Kaneoka, Hidenori; Kidani, Shunsuke; Miyake, Katsuhide; Iijima, Shinji

doi:10.1016/j.bbrc.2013.07.013

Cited by 11 publications

(9 citation statements)

References 29 publications

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“…2). The depletion of Pc2 had no effect on the excision of 6-4PPs, but hampered the repair of CPDs; 60 % of CPDs remained 24 h post irradiation, similar to PIASy knockdown as described previously (Tsuge et al 2013). The knockdown of PIAS1 led to a significant reduction in the repair of both 6-4PPs and CPDs; 35 % of 6-4PPs remained 6 h post UV irradiation, while 60 % of CPDs remained 24 h post irradiation.…”

Section: Several Sumo E3 Ligases Affected Repair Of Cpds and 6-4pps Isupporting

confidence: 80%

“…Since Pc2 has intrinsic SUMO E3 activity, CPD-repair specific proteins such as DDB2 were expected to be SUMOylated by Pc2. However, we could not detect the SUMOylation of DDB2 by Pc2 under physiological conditions (Tsuge et al 2013). This does not rule out the possibility that an unidentified protein involved in the repair of CPDs was SUMOylated.…”

Section: Discussionmentioning

confidence: 92%

“…We previously reported that DDB2 was SUMOylated by the E3 ligase PIASy in response to UV irradiation, and PIASy knockdown reduced the removal of CPDs, but not 6-4PPs (Tsuge et al 2013). In the present study, we performed RNA interference (RNAi) screening on SUMO E3 ligases to reveal the framework of SUMOylation and its importance in NER.…”

Section: Introductionmentioning

confidence: 89%

“…1 demonstrated that many proteins in chromatin were SUMOylated; however, the implication of these proteins and their SUMOylation remains unclear. We previously demonstrated the involvement of PIASy in NER (Tsuge et al 2013). Only six typical SUMO E3 ligases have been reported so far (Johnson 2004).…”

Section: Several Sumo E3 Ligases Affected Repair Of Cpds and 6-4pps Imentioning

confidence: 99%

“…The siRNA sequence for PIASy was 5 0 -GGAGUAAGAGUGGACUGAA -3 0 . The sequences of other siRNAs used were described previously (Tsuge et al 2013). …”

Section: Knockdown Of E3 Ligasesmentioning

confidence: 99%

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Implication of SUMO E3 ligases in nucleotide excision repair

et al. 2014

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Post-translational modifications alter protein function to mediate complex hierarchical regulatory processes that are crucial to eukaryotic cellular function. The small ubiquitin-like modifier (SUMO) is an important post-translational modification that affects transcriptional regulation, nuclear localization, and the maintenance of genome stability. Nucleotide excision repair (NER) is a very versatile DNA repair system that is essential for protection against ultraviolet (UV) irradiation. The deficiencies in NER function remarkably increase the risk of skin cancer. Recent studies have shown that several NER factors are SUMOylated, which influences repair efficiency. However, how SUMOylation modulates NER has not yet been elucidated. In the present study, we performed RNAi knockdown of SUMO E3 ligases and found that, in addition to PIASy, the polycomb protein Pc2 affected the repair of cyclobutane pyrimidine dimers. PIAS1 affected both the removal of 6-4 pyrimidine pyrimidone photoproducts and cyclobutane pyrimidine dimers, whereas other SUMO E3 ligases did not affect the removal of either UV lesion.

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Section: Several Sumo E3 Ligases Affected Repair Of Cpds and 6-4pps Isupporting

confidence: 80%

Section: Discussionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 89%

Section: Several Sumo E3 Ligases Affected Repair Of Cpds and 6-4pps Imentioning

confidence: 99%

“…The siRNA sequence for PIASy was 5 0 -GGAGUAAGAGUGGACUGAA -3 0 . The sequences of other siRNAs used were described previously (Tsuge et al 2013). …”

Section: Knockdown Of E3 Ligasesmentioning

confidence: 99%

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Implication of SUMO E3 ligases in nucleotide excision repair

et al. 2014

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A protein with broad functions: damage-specific DNA-binding protein 2

2022

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Damage-specific DNA-binding protein 2 (DDB2) was initially identified as a component of the damage-specific DNA-binding heterodimeric complex, which cooperates with other proteins to repair UV-induced DNA damage. DDB2 is involved in the occurrence and development of cancer by affecting nucleotide excision repair (NER), cell apoptosis, and premature senescence. DDB2 also affects the sensitivity of cancer cells to radiotherapy and chemotherapy. In addition, a recent study found that DDB2 is a pathogenic gene for hepatitis and encephalitis. In recent years, there have been few relevant literature reports on DDB2, so there is still room for further research about it. In this paper, the molecular mechanisms of different biological processes involving DDB2 are reviewed in detail to provide theoretical support for research on drugs that can target DDB2.

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