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First published online November 4, 2009
doi: 10.1242/jcs.056127

Journal of Cell Science 122, 3837-3850 (2009)
Published by The Company of Biologists 2009
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Commentary

PIP5K-driven PtdIns(4,5)P2 synthesis: regulation and cellular functions

Iman van den Bout and Nullin Divecha

Inositide Laboratory, Paterson Institute for Cancer Research, Wilmslow Road, Manchester M20 4BX, UK

ivbout{at}picr.man.ac.uk; ndivecha{at}picr.man.ac.uk

It has long been known that phosphoinositides are present in cellular membranes, but only in the past four decades has our understanding of their importance for proper cell function advanced significantly. Key to determining the biological roles of phosphoinositides is understanding the enzymes involved in their metabolism. Although many such enzymes have now been identified, there is still much to learn about their cellular functions. Phosphatidylinositol 4-phosphate 5-kinases (PIP5Ks) are a group of kinases that catalyse the production of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2]. As well as being a substrate for the enzymes phospholipase C (PLC) and phosphatidylinositol 3-kinase (PI3K), PtdIns(4,5)P2 acts as a second messenger in its own right, influencing a variety of cellular processes. In this Commentary, we review how PIP5Ks are modulated to achieve regulated PtdIns(4,5)P2 production, and discuss the role of these proteins in different cellular processes.

Key words: PIP5K1, PIP5K, PtdIns(4,5)P2, Phosphatidylinositol, Phosphatidylinositol (4,5)-bisphosphate, Phosphatidylinositol 4-phosphate 5-kinase


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