Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling |
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Authors: | Nagano Junko Kitamura Kenichiro Hujer Kristine M Ward Christopher J Bram Richard J Hopfer Ulrich Tomita Kimio Huang Chunfa Miller R Tyler |
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Institution: | Division of Nephrology, Department of Medicine, Case Western Reserve University, Lois Stokes Veterans Affairs Medical Center, Cleveland, OH, USA. |
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Abstract: | 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. |
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Keywords: | ARPKD Fibrocystin CAML Ca2+signaling Cilia PKD1 PKD2 |
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