p85 binds to G-actin in a Ca2+/calmodulin-dependent manner, thus regulating the initiation of cytokinesis in Tetrahymena

Kohsuke Gonda, Osamu Numata

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

Tetrahymena p85 is localized to the presumptive division plane before the formation of contractile ring microfilaments. p85 binds to calmodulin in a Ca2+-dependent manner and both proteins colocalize to the division furrow. Inhibition of the binding of p85 and Ca2+/calmodulin prevents both the localization of p85 and calmodulin to the division plane and the formation of the contractile ring, suggesting that the interaction of p85 and Ca2+/calmodulin is important in the formation of the contractile ring. We investigated the mechanisms of the formation of contractile ring, and the relationship among p85, CaM, and actin using co-sedimentation assay: p85 binds to G-actin in a Ca2+/calmodulin-dependent manner, but does not bind to F-actin. Therefore, we propose that a Ca2+/calmodulin signal and its target protein p85 are cooperatively involved in the recruitment of G-actin to the division plane and the formation of the contractile ring.

Original languageEnglish
Pages (from-to)1098-1103
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume292
Issue number4
DOIs
Publication statusPublished - 2002

Keywords

  • Actin
  • Actin-binding protein
  • Ca
  • Calmodulin
  • Contractile ring
  • Cytokinesis
  • Division plane
  • Microfilament
  • p85
  • Tetrahymena

Fingerprint

Dive into the research topics of 'p85 binds to G-actin in a Ca2+/calmodulin-dependent manner, thus regulating the initiation of cytokinesis in Tetrahymena'. Together they form a unique fingerprint.

Cite this