RNF168 E3 ligase participates in ubiquitin signaling and recruitment of SLX4 during DNA crosslink repair.
Sign Up to like & getrecommendations! Published in 2021 at "Cell reports"
DOI: 10.1016/j.celrep.2021.109879
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… read more here.
Keywords: dna; slx4; rnf168 ligase; recruitment slx4 ... See more keywords
PARP1 modulates telomere sister chromatid exchange and telomere length homeostasis by regulating telomere localization of SLX4 in U2OS cells.
Sign Up to like & getrecommendations! Published in 2021 at "Life sciences"
DOI: 10.1016/j.lfs.2021.119556
Abstract: OBJECTIVE Poly(ADP-ribose) polymerase-1 (PARP1) interacts and poly(ADP-ribosyl)ates telomere repeat binding factor 2 (TRF2), which acts as a platform to recruit a large number of proteins at the telomere. Since the discovery of TRF2-SLX4 interaction, SLX4… read more here.
Keywords: telomere localization; slx4; telomere length; u2os cells ... See more keywords
RNF4 and USP7 coordinate spatial regulation of SLX4 stability within the PML nuclear bodies
Sign Up to like & getrecommendations! Published in 2025 at "Nucleic Acids Research"
DOI: 10.1093/nar/gkaf941
Abstract: Abstract To protect the genome from the formation of DNA breaks by nucleases involved in DNA repair, cells have evolved multiple levels of regulatory strategies. One key regulator of nuclease activity is the scaffold protein… read more here.
Keywords: slx4 stability; within pml; nuclear bodies; slx4 ... See more keywords