Phospholipase D signaling: orchestration by PIP2 and small GTPases

Hydrolysis of phosphatidylcholine by phospholipase D (PLD) leads to the generation of the versatile lipid second messenger, phosphatidic acid (PA), which is involved in fundamental cellular processes, including membrane trafficking, actin cytoskeleton remodeling, cell proliferation and cell survival...

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Vydané v:Naunyn-Schmiedeberg's archives of pharmacology Ročník 374; číslo 5-6; s. 399 - 411
Hlavní autori: Oude Weernink, Paschal A, López de Jesús, Maider, Schmidt, Martina
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: Germany Springer-Verlag 01.02.2007
Predmet:
Animals
Biological Transport
Humans
Models, Biological
Monomeric GTP-Binding Proteins - metabolism
Phosphatidylinositol 4,5-Diphosphate - metabolism
Phospholipase D - metabolism
Phosphotransferases (Alcohol Group Acceptor) - metabolism
Review
rho GTP-Binding Proteins - metabolism
Signal Transduction
ISSN:0028-1298, 1432-1912
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Shrnutí:Hydrolysis of phosphatidylcholine by phospholipase D (PLD) leads to the generation of the versatile lipid second messenger, phosphatidic acid (PA), which is involved in fundamental cellular processes, including membrane trafficking, actin cytoskeleton remodeling, cell proliferation and cell survival. PLD activity can be dramatically stimulated by a large number of cell surface receptors and is elaborately regulated by intracellular factors, including protein kinase C isoforms, small GTPases of the ARF, Rho and Ras families and, particularly, by the phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PIP(2)). PIP(2) is well known as substrate for the generation of second messengers by phospholipase C, but is now also understood to recruit and/or activate a variety of actin regulatory proteins, ion channels and other signaling proteins, including PLD, by direct interaction. The synthesis of PIP(2) by phosphoinositide 5-kinase (PIP5K) isoforms is tightly regulated by small GTPases and, interestingly, by PA as well, and the concerted formation of PIP(2) and PA has been shown to mediate receptor-regulated cellular events. This review highlights the regulation of PLD by membrane receptors, and describes how the close encounter of PLD and PIP5K isoforms with small GTPases permits the execution of specific cellular functions.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ObjectType-Review-3
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ISSN:0028-1298
1432-1912
DOI:10.1007/s00210-007-0131-4