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

J Cell Sci. 2009 Nov 1;122(Pt 21):3837-50. doi: 10.1242/jcs.056127.

Abstract

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)P(2)]. As well as being a substrate for the enzymes phospholipase C (PLC) and phosphatidylinositol 3-kinase (PI3K), PtdIns(4,5)P(2) 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)P(2) production, and discuss the role of these proteins in different cellular processes.

Publication types

  • Review

MeSH terms

  • Animals
  • Gene Expression Regulation, Enzymologic*
  • Humans
  • Multigene Family
  • Phosphatidylinositol 4,5-Diphosphate / metabolism*
  • Phosphotransferases (Alcohol Group Acceptor) / genetics*
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism*

Substances

  • Phosphatidylinositol 4,5-Diphosphate
  • Phosphotransferases (Alcohol Group Acceptor)
  • 1-phosphatidylinositol-4-phosphate 5-kinase