Abstract
Employing a yeast two-hybrid screen with the COOH terminus of polycystin-2, one of the proteins mutated in patients with polycystic kidney disease, we were able to isolate a novel protein that we call PIGEA-14 ( polycystin-2 interactor, Golgi- and endoplasmic reticulum-associated protein with a molecular mass of 14 kDa). Molecular modeling only predicts a coiled-coil motif, but no other ...
Abstract
Employing a yeast two-hybrid screen with the COOH terminus of polycystin-2, one of the proteins mutated in patients with polycystic kidney disease, we were able to isolate a novel protein that we call PIGEA-14 ( polycystin-2 interactor, Golgi- and endoplasmic reticulum-associated protein with a molecular mass of 14 kDa). Molecular modeling only predicts a coiled-coil motif, but no other functional domains, in PIGEA-14. In a subsequent two-hybrid screen using PIGEA-14 as a bait, we found GM130, a component of the cis-compartment of the Golgi apparatus. Co-expression of the PIGEA-14 and PKD2 cDNAs in LLC-PK1 and HeLa cells resulted in a redistribution of PIGEA-14 and polycystin-2 to the trans-Golgi network, which suggests that PIGEA-14 plays an important role in regulating the intracellular location of polycystin-2 and possibly other intracellular proteins. Our results also indicate that the intracellular trafficking of polycystin-2 is regulated both at the level of the endoplasmic reticulum and that of the trans-Golgi network.
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