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Polycystin-1 is a large membrane protein that is transmitted to the primary cilia and tip surface of polarized LLC-PK1 kidney epithelial cells. Polycystin-1 undergoes cleavage to generate an N-terminal fragment that maintains non-covalent binding to the transmembrane C-terminal fragment. Exposing cells to alkaline pH will destroy binding and remove N-terminal fragments. We conducted this study at the same time and revealed that at least a part of newly synthesized polycystin-1 is transferred to cilia via the Golgi bypass route. The polycystin-1 protein undergoes autocatalytic cleavage and releases its large extracellular N-terminal domain, which remains noncovalently bound to its transmembrane domain. Exposure of the cells to the alkaline pH strip left an N-terminal domain and this property was used in experiments designed to investigate post-synthesis transport of polycystin-1. As the apical membrane pool of proteins passes through the Golgi complex, the ciliary pool appears to pursue the Golgi bypass pathway.

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