Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling

Junko Nagano, Kenichiro Kitamura, Kristine M. Hujer, Christopher J. Ward, Richard J. Bram, Ulrich Hopfer, Kimio Tomita, Chunfa Huang, R. Tyler Miller

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


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 Ca2+ 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 Ca2+ in the distal nephron in a manner similar to PKD1 and PKD2 that are involved in autosomal dominant polycystic kidney disease.

Original languageEnglish (US)
Pages (from-to)880-889
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Dec 16 2005


  • CAML
  • Casignaling
  • Cilia
  • Fibrocystin
  • PKD1
  • PKD2

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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