Figure S2. (A) ERAD and vacuole-dependent degradation of SZ* was assayed by cycloheximide chase after treatment with the proteasomal inhibitor MG132 or ...
Supplemental Materials Molecular Biology of the Cell
Sun et al.
Supplementary Materials
Figure S1. (A) The potential ERAD dependence of SZ was assayed by cycloheximide chase after treatment with the proteasomal inhibitor MG132 or the vehicle DMSO. (B) The stability of SZ* in both wild-type and kar2-1 strains was determined by cycloheximide chase analysis. Data represent means ±SE of three independent experiments.
Figure S2. (A) ERAD and vacuole-dependent degradation of SZ* was assayed by cycloheximide chase after treatment with the proteasomal inhibitor MG132 or the vehicle DMSO in pdr5ΔPEP4 and pep4Δpdr5Δ yeast. Data represent the means ±SE of three independent experiments. (B) The stability of SZ* in wild-type and the indicated autophagy defective mutants was determined by cycloheximide chase analysis.
Figure S3. (A) ERAD dependence of GFP tagged SZ* was assayed by cycloheximide chase in wild-type and mutant yeast lacking ER-resident E3 ligases HRD1 and/or DOA10. Apparent differences in degradation rate between the strains were not statistically significant. (B) Stability of SZ* in wild-type and an endocytosis defective mutant was determined by cycloheximide chase analysis. Data represent means ±SE of three independent experiments.
Figure S4. (A) Heat-shock induction was measured in a reporter assay that assesses beta-galactosidase activity. (B-C) The ERAD dependence of SZ* with constitutive HSR induction was assayed by measuring both (B) steady-state levels and (C) by a cycloheximide chase assay. Data represent means ±SE of three independent experiments. ** denotes p
