| First Author | Nagano J | Year | 2005 |
| Journal | Biochem Biophys Res Commun | Volume | 338 |
| Issue | 2 | Pages | 880-9 |
| PubMed ID | 16243292 | Mgi Jnum | J:102836 |
| Mgi Id | MGI:3608147 | Doi | 10.1016/j.bbrc.2005.10.022 |
| Citation | Nagano J, et al. (2005) Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling. Biochem Biophys Res Commun 338(2):880-9 |
| abstractText | The predicted structure of the autosomal recessive polycystic kidney disease protein, fibrocystin, suggests that it may function as a receptor, but its function remains unknown. To understand its function, we searched for proteins that interact with the intracellular C-terminus of fibrocystin using the yeast two-hybrid system. From the screening, we found calcium modulating cyclophilin ligand (CAML), a protein involved in Ca(2+) signaling. Immunofluorescent analysis showed that both proteins are co-localized in the apical membrane, primary cilia, and the basal body of cells derived from the distal nephron Epitope-tagged expression constructs of both proteins were co-immunoprecipitated from COS7 cells. The intracellular C-terminus of fibrocystin interacts with CAML, a protein with an intracellular distribution that is similar to that of PKD2. Fibrocystin may participate in regulation of intracellular Ca(2+) in the distal nephron in a manner similar to PKD1 and PKD2 that are involved in autosomal dominant polycystic kidney disease. |
