The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks

Simon Bekker-Jensen; Niels Mailand

doi:10.1016/j.febslet.2011.05.056

The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks

89 Citations (Scopus)

Abstract

DNA double-strand breaks (DSBs) represent the most destructive type of chromosomal lesion and trigger rapid chromatin restructuring accompanied by accumulation of proteins in the vicinity of the DSB. Non-proteolytic ubiquitylation of chromatin surrounding DSBs, mediated by the RNF8/RNF168 ubiquitin ligase cascade, has emerged as a key mechanism for restoration of genome integrity by licensing the DSB-modified chromatin to concentrate genome caretaker proteins such as 53BP1 and BRCA1 near the lesions. In parallel, SUMOylation of upstream DSB regulators is also required for execution of this ubiquitin-dependent chromatin response, but its molecular basis is currently unclear. Here, we discuss recent insights into how ubiquitin- and SUMO-dependent signaling processes cooperate to orchestrate protein interactions with sites of DNA damage to facilitate DSB repair.

Original language	English
Journal	FEBS Letters
Volume	585
Pages (from-to)	2914-2919
Number of pages	6
DOIs	https://doi.org/10.1016/j.febslet.2011.05.056
Publication status	Published - 16 Sept 2011

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title = "The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks",

abstract = "DNA double-strand breaks (DSBs) represent the most destructive type of chromosomal lesion and trigger rapid chromatin restructuring accompanied by accumulation of proteins in the vicinity of the DSB. Non-proteolytic ubiquitylation of chromatin surrounding DSBs, mediated by the RNF8/RNF168 ubiquitin ligase cascade, has emerged as a key mechanism for restoration of genome integrity by licensing the DSB-modified chromatin to concentrate genome caretaker proteins such as 53BP1 and BRCA1 near the lesions. In parallel, SUMOylation of upstream DSB regulators is also required for execution of this ubiquitin-dependent chromatin response, but its molecular basis is currently unclear. Here, we discuss recent insights into how ubiquitin- and SUMO-dependent signaling processes cooperate to orchestrate protein interactions with sites of DNA damage to facilitate DSB repair.",

author = "Simon Bekker-Jensen and Niels Mailand",

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year = "2011",

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doi = "10.1016/j.febslet.2011.05.056",

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T1 - The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks

AU - Bekker-Jensen, Simon

AU - Mailand, Niels

PY - 2011/9/16

Y1 - 2011/9/16

N2 - DNA double-strand breaks (DSBs) represent the most destructive type of chromosomal lesion and trigger rapid chromatin restructuring accompanied by accumulation of proteins in the vicinity of the DSB. Non-proteolytic ubiquitylation of chromatin surrounding DSBs, mediated by the RNF8/RNF168 ubiquitin ligase cascade, has emerged as a key mechanism for restoration of genome integrity by licensing the DSB-modified chromatin to concentrate genome caretaker proteins such as 53BP1 and BRCA1 near the lesions. In parallel, SUMOylation of upstream DSB regulators is also required for execution of this ubiquitin-dependent chromatin response, but its molecular basis is currently unclear. Here, we discuss recent insights into how ubiquitin- and SUMO-dependent signaling processes cooperate to orchestrate protein interactions with sites of DNA damage to facilitate DSB repair.

AB - DNA double-strand breaks (DSBs) represent the most destructive type of chromosomal lesion and trigger rapid chromatin restructuring accompanied by accumulation of proteins in the vicinity of the DSB. Non-proteolytic ubiquitylation of chromatin surrounding DSBs, mediated by the RNF8/RNF168 ubiquitin ligase cascade, has emerged as a key mechanism for restoration of genome integrity by licensing the DSB-modified chromatin to concentrate genome caretaker proteins such as 53BP1 and BRCA1 near the lesions. In parallel, SUMOylation of upstream DSB regulators is also required for execution of this ubiquitin-dependent chromatin response, but its molecular basis is currently unclear. Here, we discuss recent insights into how ubiquitin- and SUMO-dependent signaling processes cooperate to orchestrate protein interactions with sites of DNA damage to facilitate DSB repair.

U2 - 10.1016/j.febslet.2011.05.056

DO - 10.1016/j.febslet.2011.05.056

M3 - Review

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SN - 1873-3468

VL - 585

SP - 2914

EP - 2919

JO - FEBS Letters

JF - FEBS Letters

ER -

The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks

Abstract

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