DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A

Bergink, Steven; Salomons, Florian A.; Hoogstraten, Deborah; Groothuis, Tom A.M.; Waard, Harm de; Wang, Junxin; Li, Yuan; Citterio, Elisabetta; Houtsmuller, Adriaan B.; Neefjes, Jacques; Hoeijmakers, Jan H.J.; Vermeulen, Wim; Dantuma, Nico P.

doi:10.1101/gad.373706

Cited by 230 publications

(240 citation statements)

References 41 publications

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“…As a control, we used an inactive ubiquitin molecule (GFP-ubiG76) that cannot be conjugated to any target (36). Because these ubiquitin mutants are tagged with GFP, the experiments were conducted with wild-type MARCH1.…”

Section: March1 Is Polyubiquitinatedmentioning

confidence: 99%

“…To investigate the type of ubiquitination taking place in these conditions, we coexpressed MARCH1 and a GFP-tagged lysineless ubiquitin (GFP-ubiK-0) that prevents further elongation of a chain once linked to the substrate (36,37). As a control, we used an inactive ubiquitin molecule (GFP-ubiG76) that cannot be conjugated to any target (36).…”

Section: March1 Is Polyubiquitinatedmentioning

confidence: 99%

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Autoregulation of MARCH1 Expression by Dimerization and Autoubiquitination

Bourgeois-Daigneault

Thibodeau

2012

The Journal of Immunology

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Some members of the membrane-associated RING-CH family of E3 ubiquitin ligases (MARCHs) are membrane-bound and target major players of the immune response. MARCH1 ubiquitinates and downregulates MHC class II expression in APCs. It is induced by IL-10 and despite a strong increase in mRNA expression in human primary monocytes, the protein remains hardly detectable. To gain insights into the posttranslational regulation of MARCH1, we investigated whether its expression is itself regulated by ubiquitination. Our results demonstrate that MARCH1 is ubiquitinated in transfected human cell lines. Polyubiquitin chain-specific Abs revealed the presence of K48-linked polyubiquitin chains. A mutant devoid of lysine residues in the N- and C-terminal regions was less ubiquitinated and had a prolonged half-life. Reduced ubiquitination was also observed for an inactive mutated form of the molecule (M1WI), suggesting that MARCH1 is capable of autoubiquitination. Immunoprecipitation and energy transfer experiments demonstrated that MARCH1 homodimerizes and also forms heterodimers with others family members. Coexpression of MARCH1 decreased the protein levels of the inactive M1WI, suggesting a transubiquitination process. Taken together, our results suggest that MARCH1 may regulate its own expression through dimerization and autoubiquitination.

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Section: March1 Is Polyubiquitinatedmentioning

confidence: 99%

Section: March1 Is Polyubiquitinatedmentioning

confidence: 99%

Autoregulation of MARCH1 Expression by Dimerization and Autoubiquitination

Bourgeois-Daigneault

Thibodeau

2012

The Journal of Immunology

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“…21 A further argument suggesting involvement of ATR in NER-related downstream signaling is the finding that ATR function is required for NER-dependent monoubquitination of histone H2A at the site of DNA damage. 22 However, the gatekeeper mechanisms responsible for phenotypes in NER progeroid mutants remain to be identified.…”

Section: Introductionmentioning

confidence: 99%

Nucleotide Excision Repair Disorders and the Balance Between Cancer and Aging

Andressoo¹,

Hoeijmakers²,

Mitchell³

2006

Cell Cycle

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“…Bmil subsequently recruited Ring1B for ubiquitination of the histone H2A (Ismail et al 2010), which may be essential for progress of the repair reaction. UV-dependent ubiquitination of the histone H2A has also been reported (Bergink et al 2006). Thus, it is possible that a similar mechanism is involved in the repair of UV lesions.…”

Section: Discussionmentioning

confidence: 99%

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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DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A

Cited by 230 publications

References 41 publications

Autoregulation of MARCH1 Expression by Dimerization and Autoubiquitination

Autoregulation of MARCH1 Expression by Dimerization and Autoubiquitination

Nucleotide Excision Repair Disorders and the Balance Between Cancer and Aging

Implication of SUMO E3 ligases in nucleotide excision repair

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