RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response

Research output: Contribution to journalJournal articleResearchpeer-review

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RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response. / Poulsen, Sara L; Hansen, Rebecca K; Wagner, Sebastian A; van Cuijk, Loes; van Belle, Gijsbert J; Streicher, Werner; Wikström, Mats; Choudhary, Chuna Ram; Houtsmuller, Adriaan B; Marteijn, Jurgen A; Bekker-Jensen, Simon; Mailand, Niels.

In: Journal of Cell Biology, Vol. 201, No. 6, 10.06.2013, p. 797-807.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Poulsen, SL, Hansen, RK, Wagner, SA, van Cuijk, L, van Belle, GJ, Streicher, W, Wikström, M, Choudhary, CR, Houtsmuller, AB, Marteijn, JA, Bekker-Jensen, S & Mailand, N 2013, 'RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response', Journal of Cell Biology, vol. 201, no. 6, pp. 797-807. https://doi.org/10.1083/jcb.201212075

APA

Poulsen, S. L., Hansen, R. K., Wagner, S. A., van Cuijk, L., van Belle, G. J., Streicher, W., ... Mailand, N. (2013). RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response. Journal of Cell Biology, 201(6), 797-807. https://doi.org/10.1083/jcb.201212075

Vancouver

Poulsen SL, Hansen RK, Wagner SA, van Cuijk L, van Belle GJ, Streicher W et al. RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response. Journal of Cell Biology. 2013 Jun 10;201(6):797-807. https://doi.org/10.1083/jcb.201212075

Author

Poulsen, Sara L ; Hansen, Rebecca K ; Wagner, Sebastian A ; van Cuijk, Loes ; van Belle, Gijsbert J ; Streicher, Werner ; Wikström, Mats ; Choudhary, Chuna Ram ; Houtsmuller, Adriaan B ; Marteijn, Jurgen A ; Bekker-Jensen, Simon ; Mailand, Niels. / RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response. In: Journal of Cell Biology. 2013 ; Vol. 201, No. 6. pp. 797-807.

Bibtex

@article{7fb427536ff549d19816e03b71cfb763,
title = "RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response",
abstract = "Protein modifications by ubiquitin and small ubiquitin-like modifier (SUMO) play key roles in cellular signaling pathways. SUMO-targeted ubiquitin ligases (STUbLs) directly couple these modifications by selectively recognizing SUMOylated target proteins through SUMO-interacting motifs (SIMs), promoting their K48-linked ubiquitylation and degradation. Only a single mammalian STUbL, RNF4, has been identified. We show that human RNF111/Arkadia is a new STUbL, which used three adjacent SIMs for specific recognition of poly-SUMO2/3 chains, and used Ubc13-Mms2 as a cognate E2 enzyme to promote nonproteolytic, K63-linked ubiquitylation of SUMOylated target proteins. We demonstrate that RNF111 promoted ubiquitylation of SUMOylated XPC (xeroderma pigmentosum C) protein, a central DNA damage recognition factor in nucleotide excision repair (NER) extensively regulated by ultraviolet (UV)-induced SUMOylation and ubiquitylation. Moreover, we show that RNF111 facilitated NER by regulating the recruitment of XPC to UV-damaged DNA. Our findings establish RNF111 as a new STUbL that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response.",
author = "Poulsen, {Sara L} and Hansen, {Rebecca K} and Wagner, {Sebastian A} and {van Cuijk}, Loes and {van Belle}, {Gijsbert J} and Werner Streicher and Mats Wikstr{\"o}m and Choudhary, {Chuna Ram} and Houtsmuller, {Adriaan B} and Marteijn, {Jurgen A} and Simon Bekker-Jensen and Niels Mailand",
year = "2013",
month = "6",
day = "10",
doi = "10.1083/jcb.201212075",
language = "English",
volume = "201",
pages = "797--807",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "6",

}

RIS

TY - JOUR

T1 - RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response

AU - Poulsen, Sara L

AU - Hansen, Rebecca K

AU - Wagner, Sebastian A

AU - van Cuijk, Loes

AU - van Belle, Gijsbert J

AU - Streicher, Werner

AU - Wikström, Mats

AU - Choudhary, Chuna Ram

AU - Houtsmuller, Adriaan B

AU - Marteijn, Jurgen A

AU - Bekker-Jensen, Simon

AU - Mailand, Niels

PY - 2013/6/10

Y1 - 2013/6/10

N2 - Protein modifications by ubiquitin and small ubiquitin-like modifier (SUMO) play key roles in cellular signaling pathways. SUMO-targeted ubiquitin ligases (STUbLs) directly couple these modifications by selectively recognizing SUMOylated target proteins through SUMO-interacting motifs (SIMs), promoting their K48-linked ubiquitylation and degradation. Only a single mammalian STUbL, RNF4, has been identified. We show that human RNF111/Arkadia is a new STUbL, which used three adjacent SIMs for specific recognition of poly-SUMO2/3 chains, and used Ubc13-Mms2 as a cognate E2 enzyme to promote nonproteolytic, K63-linked ubiquitylation of SUMOylated target proteins. We demonstrate that RNF111 promoted ubiquitylation of SUMOylated XPC (xeroderma pigmentosum C) protein, a central DNA damage recognition factor in nucleotide excision repair (NER) extensively regulated by ultraviolet (UV)-induced SUMOylation and ubiquitylation. Moreover, we show that RNF111 facilitated NER by regulating the recruitment of XPC to UV-damaged DNA. Our findings establish RNF111 as a new STUbL that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response.

AB - Protein modifications by ubiquitin and small ubiquitin-like modifier (SUMO) play key roles in cellular signaling pathways. SUMO-targeted ubiquitin ligases (STUbLs) directly couple these modifications by selectively recognizing SUMOylated target proteins through SUMO-interacting motifs (SIMs), promoting their K48-linked ubiquitylation and degradation. Only a single mammalian STUbL, RNF4, has been identified. We show that human RNF111/Arkadia is a new STUbL, which used three adjacent SIMs for specific recognition of poly-SUMO2/3 chains, and used Ubc13-Mms2 as a cognate E2 enzyme to promote nonproteolytic, K63-linked ubiquitylation of SUMOylated target proteins. We demonstrate that RNF111 promoted ubiquitylation of SUMOylated XPC (xeroderma pigmentosum C) protein, a central DNA damage recognition factor in nucleotide excision repair (NER) extensively regulated by ultraviolet (UV)-induced SUMOylation and ubiquitylation. Moreover, we show that RNF111 facilitated NER by regulating the recruitment of XPC to UV-damaged DNA. Our findings establish RNF111 as a new STUbL that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response.

U2 - 10.1083/jcb.201212075

DO - 10.1083/jcb.201212075

M3 - Journal article

C2 - 23751493

VL - 201

SP - 797

EP - 807

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 6

ER -

ID: 46407154