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Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis.
J Biochem 2006; 140(6):785-91JB

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), PLCdelta1, PLCdelta3 and PLCbeta1, are localized to the cleavage furrow during cytokinesis. Targeting of the delta1 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.

Authors+Show Affiliations

Laboratory of Biological Signaling, Graduate School of Life Science, University of Hyogo, Harima Science Garden City, Hyogo 678-1297.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17041247

Citation

Naito, Yoko, et al. "Phospholipase C Isoforms Are Localized at the Cleavage Furrow During Cytokinesis." Journal of Biochemistry, vol. 140, no. 6, 2006, pp. 785-91.
Naito Y, Okada M, Yagisawa H. Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. J Biochem. 2006;140(6):785-91.
Naito, Y., Okada, M., & Yagisawa, H. (2006). Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. Journal of Biochemistry, 140(6), pp. 785-91.
Naito Y, Okada M, Yagisawa H. Phospholipase C Isoforms Are Localized at the Cleavage Furrow During Cytokinesis. J Biochem. 2006;140(6):785-91. PubMed PMID: 17041247.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. AU - Naito,Yoko, AU - Okada,Masashi, AU - Yagisawa,Hitoshi, Y1 - 2006/10/14/ PY - 2006/10/17/pubmed PY - 2007/2/27/medline PY - 2006/10/17/entrez SP - 785 EP - 91 JF - Journal of biochemistry JO - J. Biochem. VL - 140 IS - 6 N2 - 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), PLCdelta1, PLCdelta3 and PLCbeta1, are localized to the cleavage furrow during cytokinesis. Targeting of the delta1 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. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/17041247/Phospholipase_C_isoforms_are_localized_at_the_cleavage_furrow_during_cytokinesis_ L2 - https://academic.oup.com/jb/article-lookup/doi/10.1093/jb/mvj209 DB - PRIME DP - Unbound Medicine ER -