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Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C

Mueller-Roeber, B and Pical, Christophe LU (2002) In Plant Physiology 130(1). p.22-46
Abstract
Phosphoinositides (PIs) constitute a minor fraction of total cellular lipids in all eukaryotic cells. They fulfill many important functions through interaction with a wide range of cellular proteins. Members of distinct inositol lipid kinase families catalyze the synthesis of these phospholipids from phosphatidylinositol. The hydrolysis of PIs involves phosphatases and isoforms of PI-specific phospholipase C. Although our knowledge of the roles played by plant PIs is clearly limited at present, there is no doubt that they are involved in many physiological processes during plant growth and development. In this review, we concentrate on inositol lipid-metabolizing enzymes from the model plant Arabidopsis for which biochemical... (More)
Phosphoinositides (PIs) constitute a minor fraction of total cellular lipids in all eukaryotic cells. They fulfill many important functions through interaction with a wide range of cellular proteins. Members of distinct inositol lipid kinase families catalyze the synthesis of these phospholipids from phosphatidylinositol. The hydrolysis of PIs involves phosphatases and isoforms of PI-specific phospholipase C. Although our knowledge of the roles played by plant PIs is clearly limited at present, there is no doubt that they are involved in many physiological processes during plant growth and development. In this review, we concentrate on inositol lipid-metabolizing enzymes from the model plant Arabidopsis for which biochemical characterization data are available, namely the inositol lipid kinases and PI-specific phospholipase Cs. The biochemical properties and structure of characterized and genome-predicted isoforms are presented and compared with those of the animal enzymes to show that the plant enzymes have some features clearly unique to this kingdom. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Plant Physiology
volume
130
issue
1
pages
22 - 46
publisher
American Society of Plant Biologists
external identifiers
  • pmid:12226484
  • wos:000178087700005
  • scopus:0036742885
ISSN
1532-2548
DOI
10.1104/pp.004770
language
English
LU publication?
yes
id
c704bf41-63a2-4d85-a4cb-55eda47a3035 (old id 328509)
date added to LUP
2007-11-16 09:37:03
date last changed
2017-10-22 03:42:57
@article{c704bf41-63a2-4d85-a4cb-55eda47a3035,
  abstract     = {Phosphoinositides (PIs) constitute a minor fraction of total cellular lipids in all eukaryotic cells. They fulfill many important functions through interaction with a wide range of cellular proteins. Members of distinct inositol lipid kinase families catalyze the synthesis of these phospholipids from phosphatidylinositol. The hydrolysis of PIs involves phosphatases and isoforms of PI-specific phospholipase C. Although our knowledge of the roles played by plant PIs is clearly limited at present, there is no doubt that they are involved in many physiological processes during plant growth and development. In this review, we concentrate on inositol lipid-metabolizing enzymes from the model plant Arabidopsis for which biochemical characterization data are available, namely the inositol lipid kinases and PI-specific phospholipase Cs. The biochemical properties and structure of characterized and genome-predicted isoforms are presented and compared with those of the animal enzymes to show that the plant enzymes have some features clearly unique to this kingdom.},
  author       = {Mueller-Roeber, B and Pical, Christophe},
  issn         = {1532-2548},
  language     = {eng},
  number       = {1},
  pages        = {22--46},
  publisher    = {American Society of Plant Biologists},
  series       = {Plant Physiology},
  title        = {Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C},
  url          = {http://dx.doi.org/10.1104/pp.004770},
  volume       = {130},
  year         = {2002},
}