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Biochem Biophys Res Commun. 2002 Apr 12;292(4):1098-103.

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

Author information

1
Institute of Biological Sciences, University of Tsukuba, Ibaraki, Tsukuba, 305-8572, Japan.

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.

PMID:
11944929
DOI:
10.1006/bbrc.2002.6777
[Indexed for MEDLINE]

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