Phosphoinositides are well-known components of cellular signal transduction pathways and, more recently, have been shown to play important roles in organelle identity and targeting determinants for various cytosolic proteins. Conversion of PtdIns into its various phosphorylated derivatives, such as PtdIns4P and PtdIns(4,5)P2, is accomplished by a series of distinct lipid kinase and lipid phosphatase activities that are localized to specific subcellular membranes. As a result, production of distinct PtdIns forms is thought to be largely dependent on the access of these enzymes to their PtdIns or PtdInsP substrates. Interestingly, an investigation of two different PIS (PtdIns synthase) isoforms by Lofke et al. in this issue of the Biochemical Journal now indicates that the ability of PtdIns to be converted into downstream PtdInsPs may depend upon the PIS isoform from which it was synthesized.
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Commentary|
June 12 2008
Investigating lipid signalling: it's all about finding the right PI
Erik Nielsen
Erik Nielsen
1
1Deparment of Molecular Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, U.S.A.
1email nielsene@umich.edu
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Publisher: Portland Press Ltd
Received:
May 15 2008
Accepted:
May 27 2008
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem J (2008) 413 (1): e5–e6.
Article history
Received:
May 15 2008
Accepted:
May 27 2008
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Citation
Erik Nielsen; Investigating lipid signalling: it's all about finding the right PI. Biochem J 1 July 2008; 413 (1): e5–e6. doi: https://doi.org/10.1042/BJ20080953
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