Fig. 7: Alternative processing of the RFP-Vps10-NG-AID lumenal domain.
From: K48-ubiquitin-dependent proteases cut-up post-ER proteins
A Percentage conversion of the indicated ubiquitinated Vps10 fusion proteins to RFPp55 upon proteasome inhibition in Fig. 5. In RBD2 (WT) strains, approximately 2 % of the reporter was converted to RFPp55, increasing to ~18 % in the absence of Rbd2. B–E Changes in RFPp55 levels, normalized to dataset average, from the indicated experiments: (B) from Fig. 5A, (C) from Fig. 5B, (D) from Fig. 5C, and (E) from Fig. 6A. A–E) Bar graphs show mean ± SD, overlaid are grey circles representing values from independent experiments (n) of yeast strains described in Supplementary Tables 1 and 4 (A, n = 3 (SCFTIR1-induced degradation RFP-Vps10-NG-AID, RNF4-RING-indced degradation of RFP-Vps10-NG-AID), 5 (SCFTIR1-induced degradation RFP-Vps10-sfGFP-DHFR-AID); B, = 3; C, n = 3; D, n = 5 (WT), 4 (Δrbd2Δddi1); E, n = 3). Statistical comparisons are indicated by numbered labels, with asterisks or “ns” as prefix to denote significant differences (p < 0.05) or not significant, respectively. Full statistical outcomes are provided in Supplementary data. Pairwise comparisons were performed using two-sided unpaired t-tests, with Holm–Šidák correction following a one-way ANOVA. F RFPp55 production in strains with and without DSC2. Source data are provided as a Source Data files.
