Phospholipase D: a lipid centric review

  title={Phospholipase D: a lipid centric review},
  author={Gary M. Jenkins and Michael A. Frohman},
  journal={Cellular and Molecular Life Sciences CMLS},
  • G. JenkinsM. Frohman
  • Published 7 September 2005
  • Biology, Chemistry, Computer Science
  • Cellular and Molecular Life Sciences CMLS
Abstract.Phospholipase D (PLD) hydrolyzes the phosphodiester bond of the glycerolipid phosphatidylcholine, resulting in the production of phosphatidic acid and free choline. Phosphatidic acid is widely considered to be the intracellular lipid mediator of many of the biological functions attributed to PLD. However, phosphatidic acid is a tightly regulated lipid in cells and can be converted to other potentially bioactive lipids, including diacylglycerol and lysophosphatidic acid. PLD activities… 

Chapter 144 – Phospholipase D

Phospholipase D in platelets and other cells

It is demonstrated that PLD in platelets seems to have much of the same properties as in other cells, which implies that knowledge on PLD from other cells can be used in identifying activation mechanisms and roles in platelet cells.

Lipid signaling on the mitochondrial surface.

Phospholipid signalling through phospholipase D and phosphatidic acid

This short review highlights various phospholipid inputs into the regulation of PLD activity and also reviews potential roles for PLD‐generated phosphatidic acid, particularly a mechanism by which the phospholipsid may participate in the process of vesicular trafficking.

Mammalian Phospholipase D: Structure, Regulation, and Physiological Function of Phospholipase D and its Link to Pathology

An overview of structures, regulatory mechanisms, and physiological functions of PLD isoforms are summarized and the emerging importance of this protein family in a wide variety of diseases is discussed, including tumor growth and metastasis, cardiovascular and cerebrovascular diseases, Alzheimer's disease, and immune responses.

Molecular Mechanisms of PLD Function in Membrane Traffic

Recent data provide a mechanistic explanation for the role PLDs play in some aspects of membrane traffic and provide an explanation for why some membrane fusion reactions require PA and some do not.

Phosphatidic acid in membrane rearrangements

The biophysical properties of PA are discussed in the context of the above four roles of PA in membrane fusion and fission.

Structure and regulation of human phospholipase D.




Sequential actions of phospholipase D and phosphatidic acid phosphohydrolase 2b generate diglyceride in mammalian cells.

The first evidence for a functional role of a type 2 PAP, PAP2b, in the metabolism of PLD-generated PA is provided, and it is found that PLD2 and P AP2b act sequentially to generate diglyceride within this specialized membrane compartment.

Dual role for phosphoinositides in regulation of yeast and mammalian phospholipase D enzymes

It is reported that mutation of the PH domains of yeast and mammalian PLD enzymes generates catalytically active PI(4,5)P2-regulated enzymes with impaired biological functions.

Regulation of eukaryotic phosphatidylinositol-specific phospholipase C and phospholipase D.

This discussion emphasizes recent advances in elucidation of the mechanisms of regulation and catalysis of the various isoforms of these enzymes, especially related to structural information now available for a phospholipase C delta isozyme.

Molecular Analysis of Mammalian Phospholipase D2*

Molecular analysis of PLD2 shows that the NH2-terminal 308 amino acids are required forPLD2’s characteristic high basal activity, and it is shown that the critical role undertaken by the conserved carboxyl terminus is unlikely to involve promoting PLD association with membrane surfaces.

Mechanism of Membrane Binding of the Phospholipase D1 PX Domain*

Electrostatic potential calculations suggest that a highly positive potential near the secondary binding site may facilitate the initial adsorption of the domain to the anionic membrane, which is followed by the binding of PtdIns(3,4,5)P3 to its binding pocket.

Phospholipase D: molecular and cell biology of a novel gene family.

Emerging evidence from recent work employing new molecular tools indicates that different PLD isoforms are localized in distinct cellular organelles, where they are likely to serve diverse functions in signal transduction, membrane vesicle trafficking and cytoskeletal dynamics.

Structural Analysis of Human Phospholipase D1*

The amino-terminal 325 amino acids are required for PKC-α activation of PLD1 but not for activation by ARF1 and RhoA, and modification of the amino terminus is compatible with PLD enzymatic function and proposed a simple model for PLD activation.