TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress. / Hoffmann, Saskia; Smedegaard, Stine; Nakamura, Kyosuke; Mortuza, Gulnahar B; Räschle, Markus; Ibañez de Opakua, Alain; Oka, Yasuyoshi; Feng, Yunpeng; Blanco, Francisco J; Mann, Matthias; Montoya, Guillermo; Groth, Anja; Bekker-Jensen, Simon; Mailand, Niels.

In: The Journal of Cell Biology, Vol. 212, No. 1, 04.01.2016, p. 63-75.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Hoffmann, S, Smedegaard, S, Nakamura, K, Mortuza, GB, Räschle, M, Ibañez de Opakua, A, Oka, Y, Feng, Y, Blanco, FJ, Mann, M, Montoya, G, Groth, A, Bekker-Jensen, S & Mailand, N 2016, 'TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress', The Journal of Cell Biology, vol. 212, no. 1, pp. 63-75. https://doi.org/10.1083/jcb.201506071

APA

Hoffmann, S., Smedegaard, S., Nakamura, K., Mortuza, G. B., Räschle, M., Ibañez de Opakua, A., ... Mailand, N. (2016). TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress. The Journal of Cell Biology, 212(1), 63-75. https://doi.org/10.1083/jcb.201506071

Vancouver

Hoffmann S, Smedegaard S, Nakamura K, Mortuza GB, Räschle M, Ibañez de Opakua A et al. TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress. The Journal of Cell Biology. 2016 Jan 4;212(1):63-75. https://doi.org/10.1083/jcb.201506071

Author

Hoffmann, Saskia ; Smedegaard, Stine ; Nakamura, Kyosuke ; Mortuza, Gulnahar B ; Räschle, Markus ; Ibañez de Opakua, Alain ; Oka, Yasuyoshi ; Feng, Yunpeng ; Blanco, Francisco J ; Mann, Matthias ; Montoya, Guillermo ; Groth, Anja ; Bekker-Jensen, Simon ; Mailand, Niels. / TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress. In: The Journal of Cell Biology. 2016 ; Vol. 212, No. 1. pp. 63-75.

Bibtex

@article{877b6725a2754a6c88f0920ab3fb028d,
title = "TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress",
abstract = "Cellular genomes are highly vulnerable to perturbations to chromosomal DNA replication. Proliferating cell nuclear antigen (PCNA), the processivity factor for DNA replication, plays a central role as a platform for recruitment of genome surveillance and DNA repair factors to replication forks, allowing cells to mitigate the threats to genome stability posed by replication stress. We identify the E3 ubiquitin ligase TRAIP as a new factor at active and stressed replication forks that directly interacts with PCNA via a conserved PCNA-interacting peptide (PIP) box motif. We show that TRAIP promotes ATR-dependent checkpoint signaling in human cells by facilitating the generation of RPA-bound single-stranded DNA regions upon replication stress in a manner that critically requires its E3 ligase activity and is potentiated by the PIP box. Consequently, loss of TRAIP function leads to enhanced chromosomal instability and decreased cell survival after replication stress. These findings establish TRAIP as a PCNA-binding ubiquitin ligase with an important role in protecting genome integrity after obstacles to DNA replication.",
author = "Saskia Hoffmann and Stine Smedegaard and Kyosuke Nakamura and Mortuza, {Gulnahar B} and Markus R{\"a}schle and {Iba{\~n}ez de Opakua}, Alain and Yasuyoshi Oka and Yunpeng Feng and Blanco, {Francisco J} and Matthias Mann and Guillermo Montoya and Anja Groth and Simon Bekker-Jensen and Niels Mailand",
note = "{\circledC} 2016 Hoffmann et al.",
year = "2016",
month = "1",
day = "4",
doi = "10.1083/jcb.201506071",
language = "English",
volume = "212",
pages = "63--75",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "1",

}

RIS

TY - JOUR

T1 - TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress

AU - Hoffmann, Saskia

AU - Smedegaard, Stine

AU - Nakamura, Kyosuke

AU - Mortuza, Gulnahar B

AU - Räschle, Markus

AU - Ibañez de Opakua, Alain

AU - Oka, Yasuyoshi

AU - Feng, Yunpeng

AU - Blanco, Francisco J

AU - Mann, Matthias

AU - Montoya, Guillermo

AU - Groth, Anja

AU - Bekker-Jensen, Simon

AU - Mailand, Niels

N1 - © 2016 Hoffmann et al.

PY - 2016/1/4

Y1 - 2016/1/4

N2 - Cellular genomes are highly vulnerable to perturbations to chromosomal DNA replication. Proliferating cell nuclear antigen (PCNA), the processivity factor for DNA replication, plays a central role as a platform for recruitment of genome surveillance and DNA repair factors to replication forks, allowing cells to mitigate the threats to genome stability posed by replication stress. We identify the E3 ubiquitin ligase TRAIP as a new factor at active and stressed replication forks that directly interacts with PCNA via a conserved PCNA-interacting peptide (PIP) box motif. We show that TRAIP promotes ATR-dependent checkpoint signaling in human cells by facilitating the generation of RPA-bound single-stranded DNA regions upon replication stress in a manner that critically requires its E3 ligase activity and is potentiated by the PIP box. Consequently, loss of TRAIP function leads to enhanced chromosomal instability and decreased cell survival after replication stress. These findings establish TRAIP as a PCNA-binding ubiquitin ligase with an important role in protecting genome integrity after obstacles to DNA replication.

AB - Cellular genomes are highly vulnerable to perturbations to chromosomal DNA replication. Proliferating cell nuclear antigen (PCNA), the processivity factor for DNA replication, plays a central role as a platform for recruitment of genome surveillance and DNA repair factors to replication forks, allowing cells to mitigate the threats to genome stability posed by replication stress. We identify the E3 ubiquitin ligase TRAIP as a new factor at active and stressed replication forks that directly interacts with PCNA via a conserved PCNA-interacting peptide (PIP) box motif. We show that TRAIP promotes ATR-dependent checkpoint signaling in human cells by facilitating the generation of RPA-bound single-stranded DNA regions upon replication stress in a manner that critically requires its E3 ligase activity and is potentiated by the PIP box. Consequently, loss of TRAIP function leads to enhanced chromosomal instability and decreased cell survival after replication stress. These findings establish TRAIP as a PCNA-binding ubiquitin ligase with an important role in protecting genome integrity after obstacles to DNA replication.

U2 - 10.1083/jcb.201506071

DO - 10.1083/jcb.201506071

M3 - Journal article

C2 - 26711499

VL - 212

SP - 63

EP - 75

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 1

ER -

ID: 152960320