Centrin controls the activity of the ciliary reversal-coupled voltage-gated Ca2+ channels Ca2+-dependently

Kohsuke Gonda, Kazunori Oami, Mihoko Takahashi

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)


In Paramecium, ciliary reversal is coupled with voltage-gated Ca2+ channels on the ciliary membrane. We previously isolated a P. caudatum mutant, cnrC, with a malfunction of the Ca2+ channels and discovered that the channel activity of cnrC was restored by transfection of the P. caudatum centrin (Pccentrin1p) gene, which encodes a member of the Ca2+-binding EF-hand protein family. In this study, we injected various mutated Pccentrin1p genes into cnrC and investigated whether these genes restore the Ca2+ channel activity of cnrC. A Pccentrin1p mutant gene lacking Ca2+ sensitivity of the third and fourth EF-hands lost the ability to restore the channel function of cnrC, and mutation of the fourth EF-hand caused more serious impairment than mutation of the third EF-hand. Moreover, a Pccentrin1p gene lacking the N-terminal 34-amino acid sequence also lost the ability to restore the channel activity. Native-PAGE analysis demonstrated that the N-terminal sequence is important for the Ca2+-dependent structural change of Pccentrin1p. These results demonstrate that Pccentrin1p Ca2+-dependently regulates the Ca2+ channel activity in vivo.

Original languageEnglish
Pages (from-to)170-176
Number of pages7
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 2007 Oct 12


  • Action potential
  • Ca-binding protein
  • Centrin
  • Ciliary reversal
  • EF-hand
  • Mutant
  • Paramecium
  • RNAi
  • Structure
  • Voltage-gated Ca channel

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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