SUMOylation promotes protective responses to DNA-protein crosslinks

Research output: Contribution to journalJournal article

Standard

SUMOylation promotes protective responses to DNA-protein crosslinks. / Borgermann, Nikoline; Ackermann, Leena; Schwertman, Petra; Hendriks, Ivo A; Thijssen, Karen; Liu, Julio Cy; Lans, Hannes; Nielsen, Michael L; Mailand, Niels.

In: E M B O Journal, Vol. 38, e101496, 2019.

Research output: Contribution to journalJournal article

Harvard

Borgermann, N, Ackermann, L, Schwertman, P, Hendriks, IA, Thijssen, K, Liu, JC, Lans, H, Nielsen, ML & Mailand, N 2019, 'SUMOylation promotes protective responses to DNA-protein crosslinks', E M B O Journal, vol. 38, e101496. https://doi.org/10.15252/embj.2019101496

APA

Borgermann, N., Ackermann, L., Schwertman, P., Hendriks, I. A., Thijssen, K., Liu, J. C., ... Mailand, N. (2019). SUMOylation promotes protective responses to DNA-protein crosslinks. E M B O Journal, 38, [e101496]. https://doi.org/10.15252/embj.2019101496

Vancouver

Borgermann N, Ackermann L, Schwertman P, Hendriks IA, Thijssen K, Liu JC et al. SUMOylation promotes protective responses to DNA-protein crosslinks. E M B O Journal. 2019;38. e101496. https://doi.org/10.15252/embj.2019101496

Author

Borgermann, Nikoline ; Ackermann, Leena ; Schwertman, Petra ; Hendriks, Ivo A ; Thijssen, Karen ; Liu, Julio Cy ; Lans, Hannes ; Nielsen, Michael L ; Mailand, Niels. / SUMOylation promotes protective responses to DNA-protein crosslinks. In: E M B O Journal. 2019 ; Vol. 38.

Bibtex

@article{b11db8dbdef541dab3027aa5faa4f775,
title = "SUMOylation promotes protective responses to DNA-protein crosslinks",
abstract = "DNA-protein crosslinks (DPCs) are highly cytotoxic lesions that obstruct essential DNA transactions and whose resolution is critical for cell and organismal fitness. However, the mechanisms by which cells respond to and overcome DPCs remain incompletely understood. Recent studies unveiled a dedicated DPC repair pathway in higher eukaryotes involving the SprT-type metalloprotease SPRTN/DVC1, which proteolytically processes DPCs during DNA replication in a ubiquitin-regulated manner. Here, we show that chemically induced and defined enzymatic DPCs trigger potent chromatin SUMOylation responses targeting the crosslinked proteins and associated factors. Consequently, inhibiting SUMOylation compromises DPC clearance and cellular fitness. We demonstrate that ACRC/GCNA family SprT proteases interact with SUMO and establish important physiological roles of Caenorhabditis elegans GCNA-1 and SUMOylation in promoting germ cell and embryonic survival upon DPC formation. Our findings provide first global insights into signaling responses to DPCs and reveal an evolutionarily conserved function of SUMOylation in facilitating responses to these lesions in metazoans that may complement replication-coupled DPC resolution processes.",
author = "Nikoline Borgermann and Leena Ackermann and Petra Schwertman and Hendriks, {Ivo A} and Karen Thijssen and Liu, {Julio Cy} and Hannes Lans and Nielsen, {Michael L} and Niels Mailand",
year = "2019",
doi = "10.15252/embj.2019101496",
language = "English",
volume = "38",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",

}

RIS

TY - JOUR

T1 - SUMOylation promotes protective responses to DNA-protein crosslinks

AU - Borgermann, Nikoline

AU - Ackermann, Leena

AU - Schwertman, Petra

AU - Hendriks, Ivo A

AU - Thijssen, Karen

AU - Liu, Julio Cy

AU - Lans, Hannes

AU - Nielsen, Michael L

AU - Mailand, Niels

PY - 2019

Y1 - 2019

N2 - DNA-protein crosslinks (DPCs) are highly cytotoxic lesions that obstruct essential DNA transactions and whose resolution is critical for cell and organismal fitness. However, the mechanisms by which cells respond to and overcome DPCs remain incompletely understood. Recent studies unveiled a dedicated DPC repair pathway in higher eukaryotes involving the SprT-type metalloprotease SPRTN/DVC1, which proteolytically processes DPCs during DNA replication in a ubiquitin-regulated manner. Here, we show that chemically induced and defined enzymatic DPCs trigger potent chromatin SUMOylation responses targeting the crosslinked proteins and associated factors. Consequently, inhibiting SUMOylation compromises DPC clearance and cellular fitness. We demonstrate that ACRC/GCNA family SprT proteases interact with SUMO and establish important physiological roles of Caenorhabditis elegans GCNA-1 and SUMOylation in promoting germ cell and embryonic survival upon DPC formation. Our findings provide first global insights into signaling responses to DPCs and reveal an evolutionarily conserved function of SUMOylation in facilitating responses to these lesions in metazoans that may complement replication-coupled DPC resolution processes.

AB - DNA-protein crosslinks (DPCs) are highly cytotoxic lesions that obstruct essential DNA transactions and whose resolution is critical for cell and organismal fitness. However, the mechanisms by which cells respond to and overcome DPCs remain incompletely understood. Recent studies unveiled a dedicated DPC repair pathway in higher eukaryotes involving the SprT-type metalloprotease SPRTN/DVC1, which proteolytically processes DPCs during DNA replication in a ubiquitin-regulated manner. Here, we show that chemically induced and defined enzymatic DPCs trigger potent chromatin SUMOylation responses targeting the crosslinked proteins and associated factors. Consequently, inhibiting SUMOylation compromises DPC clearance and cellular fitness. We demonstrate that ACRC/GCNA family SprT proteases interact with SUMO and establish important physiological roles of Caenorhabditis elegans GCNA-1 and SUMOylation in promoting germ cell and embryonic survival upon DPC formation. Our findings provide first global insights into signaling responses to DPCs and reveal an evolutionarily conserved function of SUMOylation in facilitating responses to these lesions in metazoans that may complement replication-coupled DPC resolution processes.

U2 - 10.15252/embj.2019101496

DO - 10.15252/embj.2019101496

M3 - Journal article

C2 - 30914427

VL - 38

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

M1 - e101496

ER -

ID: 216015963