Fig. 4: RNF114 elongates ADPr-Ub via K11 linkage.
From: Identification of RNF114 as ADPr-Ub reader through non-hydrolysable ubiquitinated ADP-ribose
a Predicted structural model of RNF114 bound to acceptor Ub and UbcH5B–Ub. The donor UbcH5BK85–UbGly76 iso-peptide bond is poised towards the acceptor UbK11. Detailed description of how the model is obtained is available in Supp. Fig. 9. RNF114 prefers to elongate Ub on K11, as shown by neutron encoded mono-Ub consumption (b) and di-Ub formation (c). Data are presented as mean values of n = 3 independent experiments ± SEM. d Panel of DUBs remove RNF114-catalysed poly-ubiquitination on biotin-ADPr-Ub probe 1. USP2 (a specific DUB) and Cezanne (K11-specific DUB) cleave the poly-ubiquitinated species completely, while OTUD2 shows minor DUB activity. Two independent experiments were repeated with similar results. Source data are provided as a Source Data file.
