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Figure 6


Fig. 6. In contrast to UPIb, UPIa forms large aggregates in the ER, and UPIb mutants that are unable to exit from the ER sediment faster than the wild-type UPIb. Total membrane fractions from 293T cells expressing UPIa (A), UPIb (B), UPIa and UPIb (C), UPIba6 (D), UPIbE102A (E), UPIba8 (F), or UPIbA7 (G) were extracted with digitonin (1.5%) in the presence of 0.5 M NaCl. Supernatant fractions obtained after differential centrifugation were layered onto glycerol gradients (8-30%) and after centrifugation (150,000 g for 15.5 hours), aliquots of the ten gradient fractions, the sample loading zone (S) and the pellet (P) were analyzed by western blotting. Antibodies against UPIa (A,C), UPIb (B,D-F) and UPII (C) were used to localize uroplakins in the glycerol gradient. Arrowheads in A indicate the sedimentation positions of albumin (66 kDa), amylase (200 kDa) and apoferritin (443 kDa) that were used to calibrate the gradient. Asterisks indicate the peak fractions of the sedimented UP-related proteins fractions.





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