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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The polycystin 1-C-terminal fragment stimulates ERK-dependent spreading of renal epithelial cells.

Polycystin 1, the product of the PKD1 gene, is mutated in autosomal dominant polycystic kidney disease, a disease characterized by renal cyst formation and progressive renal failure. We show that expression of the C-terminal domain of human polycystin-1 (PKD1-CT) triggers spreading of isolated inner medullary collecting duct cells, a process mediated by Erk. As inner medullary collecting duct cells spread, PKD1-CT localizes to cell-extracellular matrix contacts, interacts with focal adhesion proteins Fak and paxillin, and stimulates Fak phosphorylation, paxillin phosphorylation, Fak-paxillin association, and formation of small focal complexes. PKD1-CT-mediated spreading requires membrane localization and the integrity of the C-terminal protein binding sites. We additionally show that Pkd1 null proximal tubule cells generated from Pkd1(flox/-):TSLargeT mice by in vitro Cre recombinase transfection demonstrate diminished spreading when compared with Pkd(flox/-) heterozygous parental cells. These findings suggest that membrane-bound PC1 has a central role in regulating morphogenic protein signaling at cell-matrix interfaces in non-confluent cells.[1]


  1. The polycystin 1-C-terminal fragment stimulates ERK-dependent spreading of renal epithelial cells. Joly, D., Ishibe, S., Nickel, C., Yu, Z., Somlo, S., Cantley, L.G. J. Biol. Chem. (2006) [Pubmed]
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