ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability

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ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability. / Haahr, Peter; Borgermann, Nikoline; Guo, Xiaohu; Typas, Dimitris; Achuthankutty, Divya; Hoffmann, Saskia; Shearer, Robert; Sixma, Titia K; Mailand, Niels.

In: Molecular Cell, Vol. 70, No. 1, 2018, p. 165-174.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Haahr, P, Borgermann, N, Guo, X, Typas, D, Achuthankutty, D, Hoffmann, S, Shearer, R, Sixma, TK & Mailand, N 2018, 'ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability', Molecular Cell, vol. 70, no. 1, pp. 165-174. https://doi.org/10.1016/j.molcel.2018.02.024

APA

Haahr, P., Borgermann, N., Guo, X., Typas, D., Achuthankutty, D., Hoffmann, S., ... Mailand, N. (2018). ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability. Molecular Cell, 70(1), 165-174. https://doi.org/10.1016/j.molcel.2018.02.024

Vancouver

Haahr P, Borgermann N, Guo X, Typas D, Achuthankutty D, Hoffmann S et al. ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability. Molecular Cell. 2018;70(1):165-174. https://doi.org/10.1016/j.molcel.2018.02.024

Author

Haahr, Peter ; Borgermann, Nikoline ; Guo, Xiaohu ; Typas, Dimitris ; Achuthankutty, Divya ; Hoffmann, Saskia ; Shearer, Robert ; Sixma, Titia K ; Mailand, Niels. / ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability. In: Molecular Cell. 2018 ; Vol. 70, No. 1. pp. 165-174.

Bibtex

@article{6e38b77b2c0c48e5aa7367eeefbf28f5,
title = "ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability",
abstract = "Deubiquitylating enzymes (DUBs) enhance the dynamics of the versatile ubiquitin (Ub) code by reversing and regulating cellular ubiquitylation processes at multiple levels. Here we discovered that the uncharacterized human protein ZUFSP (zinc finger with UFM1-specific peptidase domain protein/C6orf113/ZUP1), which has been annotated as a potentially inactive UFM1 protease, and its fission yeast homolog Mug105 define a previously unrecognized class of evolutionarily conserved cysteine protease DUBs. Human ZUFSP selectively interacts with and cleaves long K63-linked poly-Ub chains by means of tandem Ub-binding domains, whereas it displays poor activity toward mono- or di-Ub substrates. In cells, ZUFSP is recruited to and regulates K63-Ub conjugates at genotoxic stress sites, promoting chromosome stability upon replication stress in a manner dependent on its catalytic activity. Our findings establish ZUFSP as a new type of linkage-selective cysteine peptidase DUB with a role in genome maintenance pathways.",
author = "Peter Haahr and Nikoline Borgermann and Xiaohu Guo and Dimitris Typas and Divya Achuthankutty and Saskia Hoffmann and Robert Shearer and Sixma, {Titia K} and Niels Mailand",
note = "Copyright {\circledC} 2018 Elsevier Inc. All rights reserved.",
year = "2018",
doi = "10.1016/j.molcel.2018.02.024",
language = "English",
volume = "70",
pages = "165--174",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "1",

}

RIS

TY - JOUR

T1 - ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability

AU - Haahr, Peter

AU - Borgermann, Nikoline

AU - Guo, Xiaohu

AU - Typas, Dimitris

AU - Achuthankutty, Divya

AU - Hoffmann, Saskia

AU - Shearer, Robert

AU - Sixma, Titia K

AU - Mailand, Niels

N1 - Copyright © 2018 Elsevier Inc. All rights reserved.

PY - 2018

Y1 - 2018

N2 - Deubiquitylating enzymes (DUBs) enhance the dynamics of the versatile ubiquitin (Ub) code by reversing and regulating cellular ubiquitylation processes at multiple levels. Here we discovered that the uncharacterized human protein ZUFSP (zinc finger with UFM1-specific peptidase domain protein/C6orf113/ZUP1), which has been annotated as a potentially inactive UFM1 protease, and its fission yeast homolog Mug105 define a previously unrecognized class of evolutionarily conserved cysteine protease DUBs. Human ZUFSP selectively interacts with and cleaves long K63-linked poly-Ub chains by means of tandem Ub-binding domains, whereas it displays poor activity toward mono- or di-Ub substrates. In cells, ZUFSP is recruited to and regulates K63-Ub conjugates at genotoxic stress sites, promoting chromosome stability upon replication stress in a manner dependent on its catalytic activity. Our findings establish ZUFSP as a new type of linkage-selective cysteine peptidase DUB with a role in genome maintenance pathways.

AB - Deubiquitylating enzymes (DUBs) enhance the dynamics of the versatile ubiquitin (Ub) code by reversing and regulating cellular ubiquitylation processes at multiple levels. Here we discovered that the uncharacterized human protein ZUFSP (zinc finger with UFM1-specific peptidase domain protein/C6orf113/ZUP1), which has been annotated as a potentially inactive UFM1 protease, and its fission yeast homolog Mug105 define a previously unrecognized class of evolutionarily conserved cysteine protease DUBs. Human ZUFSP selectively interacts with and cleaves long K63-linked poly-Ub chains by means of tandem Ub-binding domains, whereas it displays poor activity toward mono- or di-Ub substrates. In cells, ZUFSP is recruited to and regulates K63-Ub conjugates at genotoxic stress sites, promoting chromosome stability upon replication stress in a manner dependent on its catalytic activity. Our findings establish ZUFSP as a new type of linkage-selective cysteine peptidase DUB with a role in genome maintenance pathways.

U2 - 10.1016/j.molcel.2018.02.024

DO - 10.1016/j.molcel.2018.02.024

M3 - Journal article

C2 - 29576528

VL - 70

SP - 165

EP - 174

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 1

ER -

ID: 194259310