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 journal › Journal article › Research › peer-review
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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