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A more recent version of this article appeared on December 1, 2002
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Submitted on April 17, 2002
Revised on August 13, 2002
Accepted on August 21, 2002
1 Department of Cell Biology, New York University, School of Medicine 550 First Avenue, New York, NY 10016
2 Ronald O. Perelman Department of Dermatology, Department of Pharmacology, Department of Urology, and Kaplan Comprehensive Cancer Center, New York University, School of Medicine 550 First Avenue, New York, NY 10016
3 Kaplan Comprehensive Cancer Center, New York University, School of Medicine 550 First Avenue, New York, NY 10016
* Corresponding author. E-mail address: kreibg01{at}endeavor.med.nyu.edu.
Much of the lower urinary tract including the bladder is lined by a stratified urothelium forming a highly differentiated, most superficial umbrella cell layer. The apical plasma membrane as well as abundant cytoplasmic fusiform vesicles of the umbrella cells is covered by two-dimensional crystals that are formed by four membrane proteins named uroplakins Ia, Ib, II and III. Uroplakins (UP) are synthesized on membrane-bound polysomes, and after several co- and post-translational modifications they assemble into planar crystals in a post-Golgi vesicular compartment. Distension of the bladder may cause fusiform vesicles to fuse with the apical plasma membrane. We have investigated the early stages of uroplakin assembly by expressing the four uroplakins in 293T cells. Transfection experiments showed that, when expressed individually, only UPIb can exit from the ER and move to the plasma membrane, while UPII and UPIII reach the plasma membrane only when they form heterodimeric complexes with UPIa and UPIb, respectively. Heterodimer formation in the ER was confirmed by pulse-chase experiment followed by co-immunoprecipitation. Our results indicate that the initial building blocks for the assembly of crystalline uroplakin plaques are heterodimeric uroplakin complexes that form in the ER.
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