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Fig. 5 | BMC Biology

Fig. 5

From: Aneuploidy-induced proteotoxic stress can be effectively tolerated without dosage compensation, genetic mutations, or stress responses

Fig. 5

Aneuploid strains show no defects in the degradation of misfolded proteins. ad Stability of misfolded substrate proteins in vivo subject to ER-associated degradation (ERAD) or cytosolic quality control (CytoQC) degradation pathways. Wild type (WT) and aneuploid strains were pulse-labeled for 10 min (CPY* and Sec61-2) or 5 min (KWS and Ste6*C) and chased for the times indicated. All proteins were immunoprecipitated using anti-HA antibodies and were resolved by SDS-PAGE and quantified using a phosphorimager. Representative phosphor screen scans are shown separated by experimental batches. Error bars represent the SD of three independent experiments except for WT which is displayed as an average of all experimental batches (N = 9 (CPY*), N = 10 (Sec61–2), N = 7 (KWS), or N = 9 (Ste6*C)). Turnover of a the ERAD luminal (ERAD-L) substrate CPY*. D1/8 (*) and D1/2/8/11 (*) are statistically different from their respective euploid controls at time 60 min (see Additional file 12: Fig. S8 for statistical comparison), b ERAD membrane (ERAD-M) substrate Sec61-2. D1/2 (**) and D1/2/8 (**) and D1/2/8/11 (*) are statistically different from their respective euploid controls at time 60 min, and c ERAD cytosolic (ERAD-C) substrate KWS. No aneuploid strains were statistically different from their respective euploid controls at time 15 min, d CytoQC substrate Ste6*C are shown. No aneuploid strains were statistically different from their respective euploid controls at time 30 min, Student’s t test: ***p < 0.001, **p < 0.01, *p < 0.05, and not significant p ≥ 0.05 is left unmarked. The following figure supplements are available for Fig. 5: Additional file 12: Fig. S8 and Additional file 13: Fig. S9

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