RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response
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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 journal › Journal article › Research › peer-review
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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