RRC ID 82837
著者 Katsuki Y, Abe M, Park SY, Wu W, Yabe H, Yabe M, van Attikum H, Nakada S, Ohta T, Seidman MM, Kim Y, Takata M.
タイトル RNF168 E3 ligase participates in ubiquitin signaling and recruitment of SLX4 during DNA crosslink repair.
ジャーナル Cell Rep
Abstract SLX4/FANCP is a key Fanconi anemia (FA) protein and a DNA repair scaffold for incision around a DNA interstrand crosslink (ICL) by its partner XPF nuclease. The tandem UBZ4 ubiquitin-binding domains of SLX4 are critical for the recruitment of SLX4 to damage sites, likely by binding to K63-linked polyubiquitin chains. However, the identity of the ubiquitin E3 ligase that mediates SLX4 recruitment remains unknown. Using small interfering RNA (siRNA) screening with a GFP-tagged N-terminal half of SLX4 (termed SLX4-N), we identify the RNF168 E3 ligase as a critical factor for mitomycin C (MMC)-induced SLX4 foci formation. RNF168 and GFP-SLX4-N colocalize in MMC-induced ubiquitin foci. Accumulation of SLX4-N at psoralen-laser ICL tracks or of endogenous SLX4 at Digoxigenin-psoralen/UVA ICL is dependent on RNF168. Finally, we find that RNF168 is epistatic with SLX4 in promoting MMC tolerance. We conclude that RNF168 is a critical component of the signal transduction that recruits SLX4 to ICL damage.
巻・号 37(4)
ページ 109879
公開日 2021-10-26
DOI 10.1016/j.celrep.2021.109879
PII S2211-1247(21)01349-8
PMID 34706224
PMC PMC11388903
MeSH DNA Repair* Digoxigenin / pharmacology Ficusin / pharmacology HCT116 Cells Humans MCF-7 Cells Mitomycin / pharmacology Recombinases / genetics Recombinases / metabolism* Signal Transduction* Ubiquitin / genetics Ubiquitin / metabolism* Ubiquitin-Protein Ligases / genetics Ubiquitin-Protein Ligases / metabolism*
IF 8.109
リソース情報
遺伝子材料 CSII-CMV-MCS-IRES2-Bsd (RDB04385)