Lipid translocation across the plasma membrane of mammalian cells

Bevers, Edouard M.; Comfurius, Paul; Dekkers, David W. C.; Zwaal, R.F.A.

doi:10.1016/s1388-1981(99)00110-9

Cited by 391 publications

(308 citation statements)

References 107 publications

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“…The outer leaflet of eukaryotic plasma membrane bilayers predominantly contains sphingomyelin and phosphatidylcholine while aminophospholipids, such as PS and phosphatidylethanolamine, are enriched in the inner leaflet. Phospholipid distribution within these outer and inner leaflets of the PM is tightly regulated by specialized enzymatic mechanisms that include "flippases", "floppases", and "scramblases" [4,5]. Loss of membrane phospholipid asymmetry, particularly PS flip from the inner to the outer leaflets, has been associated with many pathologic conditions.…”

Section: P2x7r-mediated Regulation Of Plasma Membrane Composition Andmentioning

confidence: 99%

P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways

Dubyak

2009

Purinergic Signalling

106

101

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Activation of the P2X7 receptor (P2X7R) triggers a remarkably diverse array of membrane trafficking responses in leukocytes and epithelial cells. These responses result in altered profiles of cell surface lipid and protein composition that can modulate the direct interactions of P2X7R-expressing cells with other cell types in the circulation, in blood vessels, at epithelial barriers, or within sites of immune and inflammatory activation. Additionally, these responses can result in the release of bioactive proteins, lipids, and large membrane complexes into extracellular compartments for remote communication between P2X7R-expressing cells and other cells that amplify or modulate inflammation, immunity, and responses to tissue damages. This review will discuss P2X7R-mediated effects on membrane composition and trafficking in the plasma membrane (PM) and intracellular organelles, as well as actions of P2X7R in controlling various modes of nonclassical secretion. It will review P2X7R regulation of: (1) phosphatidylserine distribution in the PM outer leaflet; (2) shedding of PM surface proteins; (3) release of PM-derived microvesicles or microparticles; (4) PM blebbing; (5) cell-cell fusion resulting in formation of multinucleate cells; (6) phagosome maturation and fusion with lysosomes; (7) permeability of endosomes with internalized pathogen-associated molecular patterns; (8) permeability/integrity of mitochondria; (9) exocytosis of secretory lysosomes; and (10) release of exosomes from multivesicular bodies.

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Section: P2x7r-mediated Regulation Of Plasma Membrane Composition Andmentioning

confidence: 99%

P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways

Dubyak

2009

Purinergic Signalling

106

101

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“…phospholipids in a nonspecific manner that eliminates the membrane asymmetry inherent to healthy cells (17,171,200). The loss of membrane phospholipid asymmetry contributes to microvesicle shedding.…”

Section: Substrates For Lppmentioning

confidence: 99%

Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

Nanjundan

Possmayer

2003

American Journal of Physiology-Lung Cellular and Molecular Phys

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The lung contains two distinct forms of phosphatidic acid phosphatase (PAP). PAP1 is a cytosolic enzyme that is activated through fatty acid-induced translocation to the endoplasmic reticulum, where it converts phosphatidic acid (PA) to diacylglycerol (DAG) for the biosynthesis of phospholipids and neutral lipids. PAP1 is Mg2+ dependent and sulfhydryl reagent sensitive. PAP2 is a six-transmembrane-domain integral protein localized to the plasma membrane. Because PAP2 degrades sphingosine-1-phosphate (S1P) and ceramide-1-phosphate in addition to PA and lyso-PA, it has been renamed lipid phosphate phosphohydrolase (LPP). LPP is Mg2+independent and sulfhydryl reagent insensitive. This review describes LPP isoforms found in the lung and their location in signaling platforms (rafts/caveolae). Pulmonary LPPs likely function in the phospholipase D pathway, thereby controlling surfactant secretion. Through lowering the levels of lyso-PA and S1P, which serve as agonists for endothelial differentiation gene receptors, LPPs regulate cell division, differentiation, apoptosis, and mobility. LPP activity could also influence transdifferentiation of alveolar type II to type I cells. It is considered likely that these lipid phosphohydrolases have critical roles in lung morphogenesis and in acute lung injury and repair.

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“…P-type ATPases are so named because of the phosphoenzyme intermediate formed during their activation and have been implicated in a number of transport and signaling processes. The best-known members of the group are H ϩ -ATPases and heavy metal transporters (for reviews, see Catty et al, 1997;Bevers et al, 1999;Nelson and Harvey, 1999). All P-type ATPases share a core structure, including the presence of a phosphorylation site, an ATP binding domain, and three other consensus sequences ( Figure 5).…”

Section: Pde1 Encodes a Putative Aminophospholipid Translocasementioning

confidence: 99%

“…The asymmetric distribution of lipids provides both sides of a membrane with different characteristics, which are necessary for their different functions. The biological consequences of losing membrane asymmetry can be significant; apoptosis, for example, is accompanied by rapid loss of phospholipid asymmetry, which is required for recognition of apoptotic cells by macrophages (Bevers et al, 1999). The regulated disruption of phospholipid asymmetry consequently provides a pathway for cellular signaling in response to physiological conditions or environmental stresses.…”

mentioning

confidence: 99%

PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

Balhadère

Talbot

2001

Plant Cell

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Plant infection by the rice blast fungus Magnaporthe grisea is brought about by the action of specialized infection cells called appressoria. These infection cells generate enormous turgor pressure, which is translated into an invasive force that allows a narrow penetration hypha to breach the plant cuticle. The Magnaporthe pde1 mutant was identified previously by restriction enzyme-mediated DNA integration mutagenesis and is impaired in its ability to elaborate penetration hyphae. Here we report that the pde1 mutation is the result of an insertion into the promoter of a P-type ATPase-encoding gene. Targeted gene disruption confirmed the role of PDE1 in penetration hypha development and pathogenicity but highlighted potential differences in PDE1 regulation in different Magnaporthe strains. The predicted PDE1 gene product was most similar to members of the aminophospholipid translocase group of P-type ATPases and was shown to be a functional homolog of the yeast ATPase gene ATC8 . Spatial expression studies showed that PDE1 is expressed in germinating conidia and developing appressoria. These findings implicate the action of aminophospholipid translocases in the development of penetration hyphae and the proliferation of the fungus beyond colonization of the first epidermal cell. INTRODUCTIONOne of the principal reasons why pathogenic fungi are so successful at causing plant disease is their ability to penetrate the plant cuticle directly, often using specialized infection cells called appressoria (Mendgen et al., 1996). A wide variety of fungal pathogens form appressoria, and the development of these cells involves a complex morphogenetic program that results in rapid differentiation of a highly specialized structure (Dean, 1997). The rice blast fungus Magnaporthe grisea is an important pathogen of cultivated rice and has emerged as an experimental model for the study of plant infection processes (for reviews, see Howard and Valent, 1996;Hamer and Talbot, 1998). Magnaporthe develops dome-shaped appressoria, which form at the ends of germ tubes soon after spore germination on the leaf surface. Appressoria attach strongly to the leaf and then generate enormous turgor pressure (up to 8 MPa), which is used to rupture the plant cuticle (Howard et al., 1991). The turgor inside appressoria is generated by a rapid increase in intracellular glycerol levels, which is maintained by a specialized cell wall layer containing melanin (Howard and Ferrari, 1989;de Jong et al., 1997). If melanin biosynthesis is blocked, either by chemical intervention or mutation, then Magnaporthe is unable to penetrate the plant surface and cannot cause disease (Chida and Sisler, 1987;Chumley and Valent, 1990).How such enormous cellular turgor is translated into the substantial invasive force necessary to breach the plant cell wall is not clear, but it appears to involve polarization of the cytoskeleton to the point of infection and localized cell wall modification Howard, 1990, 1992;Bechinger et al., 1999). A narrow penetration hypha forms at t...

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Lipid translocation across the plasma membrane of mammalian cells

Cited by 391 publications

References 107 publications

P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways

P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways

Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

PDE1 Encodes a P-Type ATPase Involved in Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe grisea

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