p85 binds to G-actin in a Ca(2+)/calmodulin-dependent manner, thus regulating the initiation of cytokinesis in tetrahymena

Biochem Biophys Res Commun. 2002 Apr 12;292(4):1098-103. doi: 10.1006/bbrc.2002.6777.

Abstract

Tetrahymena p85 is localized to the presumptive division plane before the formation of contractile ring microfilaments. p85 binds to calmodulin in a Ca(2+)-dependent manner and both proteins colocalize to the division furrow. Inhibition of the binding of p85 and Ca(2+)/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 Ca(2+)/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 Ca(2+)/calmodulin-dependent manner, but does not bind to F-actin. Therefore, we propose that a Ca(2+)/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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton
  • Actins / chemistry
  • Actins / metabolism*
  • Animals
  • Calcium / metabolism*
  • Calmodulin / chemistry
  • Calmodulin / metabolism*
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism*
  • Cell Division / physiology
  • Electrophoresis, Polyacrylamide Gel
  • Protein Binding / physiology
  • Protozoan Proteins*
  • Signal Transduction / physiology
  • Tetrahymena / cytology
  • Tetrahymena / metabolism*

Substances

  • Actins
  • Calmodulin
  • Cell Cycle Proteins
  • Protozoan Proteins
  • p85 protein, Tetrahymena
  • Calcium