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Journal of Biochemistry Advance Access originally published online on October 14, 2006
Journal of Biochemistry 2006 140(6):785-791; doi:10.1093/jb/mvj209
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© 2006 The Japanese Biochemical Society.

ARTICLE

Phospholipase C Isoforms Are Localized at the Cleavage Furrow during Cytokinesis

Yoko Naito*, Masashi Okada*,{dagger} and Hitoshi Yagisawa{ddagger}

Laboratory of Biological Signaling, Graduate School of Life Science, University of Hyogo, Harima Science Garden City, Hyogo 678-1297

{ddagger} To whom correspondence should be addressed. Tel: +81-791-58-0198, Fax: +81-791-58-0198, E-mail: yagisawa{at}sci.u-hyogo.ac.jp


  Abstract

It has recently been demonstrated that phosphatidylinositol 4,5-bisphosphate (PIP2) is localized at the cleavage furrow in dividing cells and its hydrolysis is required for complete cytokinesis, suggesting a pivotal role of PIP2 in cytokinesis. Here, we report that at least three mammalian isoforms of phosphoinositide-specific phospholipase C (PLC), PLC{delta}1, PLC{delta}3 and PLCß1, are localized to the cleavage furrow during cytokinesis. Targeting of the {delta}1 isoform to the furrow depends on the specific interaction between the PH domain and PIP2 in the plasma membrane. The necessity of active PLC in animal cell cytokinesis was confirmed using the specific inhibitors for PIP2 hydrolysis. These results support the model that activation of selected PLC isoforms at the cleavage furrow controls progression of cytokinesis through regulation of PIP2 levels: induction of the cleavage furrow by a contractile ring consisting of actomyosin is regulated by PIP2-dependent actin-binding proteins and formation of specific lipid domains required for membrane separation is affected by alterations in the lipid composition of the furrow.

* Contributed equally to this work.

{dagger} Present address: Department of Pathology, Laboratory Medicine, Emory University School of Medicine, 615 Michael Street, Atlanta GA 30322, USA.


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