Ubiquitylation at Stressed Replication Forks: Mechanisms and Functions

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Ubiquitylation at Stressed Replication Forks : Mechanisms and Functions. / Mirsanaye, Ann Schirin; Typas, Dimitris; Mailand, Niels.

In: Trends in Cell Biology, Vol. 31, No. 7, 2021, p. 584-597.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Mirsanaye, AS, Typas, D & Mailand, N 2021, 'Ubiquitylation at Stressed Replication Forks: Mechanisms and Functions', Trends in Cell Biology, vol. 31, no. 7, pp. 584-597. https://doi.org/10.1016/j.tcb.2021.01.008

APA

Mirsanaye, A. S., Typas, D., & Mailand, N. (2021). Ubiquitylation at Stressed Replication Forks: Mechanisms and Functions. Trends in Cell Biology, 31(7), 584-597. https://doi.org/10.1016/j.tcb.2021.01.008

Vancouver

Mirsanaye AS, Typas D, Mailand N. Ubiquitylation at Stressed Replication Forks: Mechanisms and Functions. Trends in Cell Biology. 2021;31(7):584-597. https://doi.org/10.1016/j.tcb.2021.01.008

Author

Mirsanaye, Ann Schirin ; Typas, Dimitris ; Mailand, Niels. / Ubiquitylation at Stressed Replication Forks : Mechanisms and Functions. In: Trends in Cell Biology. 2021 ; Vol. 31, No. 7. pp. 584-597.

Bibtex

@article{5634c28b626e41c0b5cd3a6196e14b76,
title = "Ubiquitylation at Stressed Replication Forks: Mechanisms and Functions",
abstract = "Accurate duplication of chromosomal DNA is vital for faithful transmission of the genome during cell division. However, DNA replication integrity is frequently challenged by genotoxic insults that compromise the progression and stability of replication forks, posing a threat to genome stability. It is becoming clear that the organization of the replisome displays remarkable flexibility in responding to and overcoming a wide spectrum of fork-stalling insults, and that these transactions are dynamically orchestrated and regulated by protein post-translational modifications (PTMs) including ubiquitylation. In this review, we highlight and discuss important recent advances on how ubiquitin-mediated signaling at the replication fork plays a crucial multifaceted role in regulating replisome composition and remodeling its configuration upon replication stress, thereby ensuring high-fidelity duplication of the genome.",
author = "Mirsanaye, {Ann Schirin} and Dimitris Typas and Niels Mailand",
note = "Copyright {\textcopyright} 2021 The Authors. Published by Elsevier Ltd.. All rights reserved.",
year = "2021",
doi = "10.1016/j.tcb.2021.01.008",
language = "English",
volume = "31",
pages = "584--597",
journal = "Trends in Cell Biology",
issn = "0962-8924",
publisher = "Elsevier Ltd. * Trends Journals",
number = "7",

}

RIS

TY - JOUR

T1 - Ubiquitylation at Stressed Replication Forks

T2 - Mechanisms and Functions

AU - Mirsanaye, Ann Schirin

AU - Typas, Dimitris

AU - Mailand, Niels

N1 - Copyright © 2021 The Authors. Published by Elsevier Ltd.. All rights reserved.

PY - 2021

Y1 - 2021

N2 - Accurate duplication of chromosomal DNA is vital for faithful transmission of the genome during cell division. However, DNA replication integrity is frequently challenged by genotoxic insults that compromise the progression and stability of replication forks, posing a threat to genome stability. It is becoming clear that the organization of the replisome displays remarkable flexibility in responding to and overcoming a wide spectrum of fork-stalling insults, and that these transactions are dynamically orchestrated and regulated by protein post-translational modifications (PTMs) including ubiquitylation. In this review, we highlight and discuss important recent advances on how ubiquitin-mediated signaling at the replication fork plays a crucial multifaceted role in regulating replisome composition and remodeling its configuration upon replication stress, thereby ensuring high-fidelity duplication of the genome.

AB - Accurate duplication of chromosomal DNA is vital for faithful transmission of the genome during cell division. However, DNA replication integrity is frequently challenged by genotoxic insults that compromise the progression and stability of replication forks, posing a threat to genome stability. It is becoming clear that the organization of the replisome displays remarkable flexibility in responding to and overcoming a wide spectrum of fork-stalling insults, and that these transactions are dynamically orchestrated and regulated by protein post-translational modifications (PTMs) including ubiquitylation. In this review, we highlight and discuss important recent advances on how ubiquitin-mediated signaling at the replication fork plays a crucial multifaceted role in regulating replisome composition and remodeling its configuration upon replication stress, thereby ensuring high-fidelity duplication of the genome.

U2 - 10.1016/j.tcb.2021.01.008

DO - 10.1016/j.tcb.2021.01.008

M3 - Review

C2 - 33612353

VL - 31

SP - 584

EP - 597

JO - Trends in Cell Biology

JF - Trends in Cell Biology

SN - 0962-8924

IS - 7

ER -

ID: 259834220