Phosphatidylinositol 5-phosphate 4-kinase γ (PI5P4Kγ), a lipid signalling enigma. (May 2016)

• Record Type: Journal Article
• Authors: Giudici, Maria-Luisa; Clarke, Jonathan H.; Irvine, Robin F.
• Is Part Of: Advances in biological regulation. Volume 61(2016)
• Page Start: 47
• Page End: 50
• Publication Date: 2016-05
• Subjects: Phosphatidylinositol 5-phosphate -- Phosphatidylinositol 5-phosphate 4-kinase γ -- PI5P -- PI5P4K -- PI5P4Kγ; PI5P phosphatidylinositol 5-phosphate -- PI(4, 5)P2 phosphatidylinositol 4, 5, -bisphosphate; Cellular control mechanisms -- Periodicals; Biological control systems -- Periodicals; Molecular biology -- Periodicals; Periodicals; 571.74
• DOI: 10.1016/j.jbior.2015.11.007
• Languages: English
• ISSNs: 2212-4926

Abstract

Abstract: The phosphatidylinositol 5-phosphate 4-kinases (PI5P4Ks) are an important family of enzymes, whose physiological roles are being teased out by a variety of means. Phosphatidylinositol-5-phosphate 4-kinase γ (PI5P4Kγ) is especially intriguing as its in vitro activity is very low. Here we review what is known about this enzyme and discuss some recent advances towards an understanding of its physiology. Additionally, the effects of the ATP-competitive inhibitor I-OMe Tyrphostin AG-538 on all three mammalian PI5P4Ks was explored, including two PI5P4Kγ mutants with altered ATP- or PI5P-binding sites. The results suggest a strategy for targeting non-ATP binding sites on inositol lipid kinases.