Stimulation of actin stress fibre formation mediated by activation of phospholipase D

Cross, Michael; Roberts, Sally; Ridley, Anne J.; Hodgkin, Matthew N.; Stewart, Allison; Welsh, Lena Claesson; Wakelam, Michael J.O.

doi:10.1016/s0960-9822(02)00545-6

Cited by 219 publications

(161 citation statements)

References 37 publications

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“…Conversely, PLD2 may function in cellular responses that contribute to phagocytosis from more distant sites, such as stimulation of PKC, which itself then translocates to the phagosome (74). Both PLD1 and PLD2 have been linked physically and functionally to the actin cytoskeleton (16,(75)(76)(77)(78)(79)(80), and each may contribute to actin's role in phagocytosis, but at different cellular sites. Such complementary, but distinctive, functions for PLD1 and PLD2 have recently been characterized in colonic epithelia (28) and mast cells (64).…”

Section: Discussionmentioning

confidence: 99%

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Barton¹,

Bourgoin²,

Kusner

2004

The Journal of Immunology

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Phagocytosis is a fundamental feature of the innate immune system, required for antimicrobial defense, resolution of inflammation, and tissue remodeling. Furthermore, phagocytosis is coupled to a diverse range of cytotoxic effector mechanisms, including the respiratory burst, secretion of inflammatory mediators and Ag presentation. Phospholipase D (PLD) has been linked to the regulation of phagocytosis and subsequent effector responses, but the identity of the PLD isoform(s) involved and the molecular mechanisms of activation are unknown. We used primary human macrophages and human THP-1 promonocytes to characterize the role of PLD in phagocytosis. Macrophages, THP-1 cells, and other human myelomonocytic cells expressed both PLD1 and PLD2 proteins. Phagocytosis of complement-opsonized zymosan was associated with stimulation of the activity of both PLD1 and PLD2, as demonstrated by a novel immunoprecipitation-in vitro PLD assay. Transfection of dominant-negative PLD1 or PLD2 each inhibited the extent of phagocytosis (by 55–65%), and their combined effects were additive (reduction of 91%). PLD1 and PLD2 exhibited distinct localizations in resting macrophages and those undergoing phagocytosis, and only PLD1 localized to the phagosome membrane. The COS-7 monkey fibroblast cell line, which has been used as a heterologous system for the analysis of receptor-mediated phagocytosis, expressed PLD2 but not PLD1. These data support a model in which macrophage phagocytosis is coordinately regulated by both PLD1 and PLD2, with isoform-specific localization. Human myelomonocytic cell lines accurately model PLD-dependent signal transduction events required for phagocytosis, but the heterologous COS cell system does not.

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Section: Discussionmentioning

confidence: 99%

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Barton¹,

Bourgoin²,

Kusner

2004

The Journal of Immunology

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“…Conversely, diminished basal and stimulated cAMP concentrations in ras-transformed cells (Tagliaferri et al, 1988;Davies et al, 1989;Wakelam et al, 1991) may result partly from the large increase in PA concentrations ( Figure 2 and Table 1) which could inhibit adenylyl cyclase (Murayama and Ui, 1987;van Corven et al, 1989;GoÂ mez-MunÄ oz et al, 1994). Increased PA concentrations in ras-transformed fibroblasts could also alter morphology since PA, or its derivative lysoPA, can activate actin polymerization involving Rho (Ha and Exton, 1993;Moolenaar, 1995;Cross et al, 1996). The decreased PAP-2 activity of the ras-transformed ®broblasts (Martin et al, 1993) could also increase the duration and magnitude of signaling by the mitogenic lipids, lysoPA, ceramide 1-phosphate and sphingosine 1-phosphate in addition to PA since PAP-2 degrades all of these lipids Brindley and Waggoner, 1996).…”

Section: Discussionmentioning

confidence: 99%

Increased concentrations of phosphatidate, diacylglycerol and ceramide in ras- and tyrosine kinase (fps)-transformed fibroblasts

et al. 1997

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Concentrations of the bioactive lipids, phosphatidate and diacylglycerol, increased with time in culture in ras-and tyrosine kinase (fps)-transformed ®broblasts but not in control ®broblasts. On Day 3, diacylglycerol and phosphatidate concentrations were about 3.3-and 5.5-fold higher respectively in the ras-transformed compared to control ®broblasts. These concentrations in fpstransformed ®broblasts were increased about twofold. The changes in phosphatidate and diacylglycerol resulted from enhanced phospholipid turnover rather than from synthesis de novo. The increased ratio of phosphatidate to diacylglycerol is explained by decreased activities of two distinct phosphatidate phosphohydrolases and increased diacylglycerol kinase in ras-transformed ®bro-blasts. Ceramide concentrations were about 2.5-and threefold higher in the fps-and ras-transformed cells respectively on Day 3 compared to the controls. Incubating control ®broblasts from Days 1 to 3 with phosphatidylcholine-speci®c phospholipase C increased diacylglycerol, phosphatidate and ceramide concentrations, and decreased Mg 2+ -independent-phosphatidate phosphohydrolase activity. 8-(4-chlorophenylthio)-cAMP had a cytostatic e ect in ras-transformed cells, it decreased the concentrations of phosphatidate and diacylglycerol, but increased that of ceramide. The consequences of increased ceramide and phosphatidate concentrations in ras-transformed cells are discussed in relation to signal transduction, cell division and the transformed phenotype.

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“…More recently, PLD activity has been found in the detergent-insoluble fraction of various cell types that contain a wide range of cytoskeletal proteins (17)(18). Several cytoskeletal proteins such as fodrin and gelsolin have been found to act as PLDspecific inhibitors in vitro (19 -21), and agonist-induced PLD stimulation can provoke changes in cell morphology through cytoskeletal rearrangement (5,(22)(23)(24). Furthermore, we reported previously that ␣-actinin, an F-actin cross-linking protein, also binds to PLD2 to inhibit its activity (25).…”

Section: Mammalian Phospholipase D (Pld)mentioning

confidence: 94%

Actin Directly Interacts with Phospholipase D, Inhibiting Its Activity

Lee

Park

Kim

et al. 2001

Journal of Biological Chemistry

105

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Mammalian phospholipase D (PLD) plays a key role in several signal transduction pathways and is involved in many diverse functions. To elucidate the complex molecular regulation of PLD, we investigated PLD-binding proteins obtained from rat brain extract. Here we report that a 43-kDa protein in the rat brain, ␤-actin, acts as a major PLD2 direct-binding protein as revealed by peptide mass fingerprinting in combination with matrixassisted laser desorption ionization/time-of-flight mass spectrometry. We also determined that the region between amino acids 613 and 723 of PLD2 is required for the direct binding of ␤-actin, using bacterially expressed glutathione S-transferase fusion proteins of PLD2 fragments. Intriguingly, purified ␤-actin potently inhibited both phosphatidylinositol-4,5-bisphosphateand oleate-dependent PLD2 activities in a concentrationdependent manner (IC 50 ‫؍‬ 5 nM). In a previous paper, we reported that ␣-actinin inhibited PLD2 activity in an interaction-dependent and an ADP-ribosylation factor 1 In vitro binding analyses showed that ␤-actin could displace ␣-actinin binding to PLD2, demonstrating independent interaction between cytoskeletal proteins and PLD2. Furthermore, ARF1 could steer the PLD2 activity in a positive direction regardless of the inhibitory effect of ␤-actin on PLD2. We also observed that ␤-actin regulates PLD1 and PLD2 with similar binding and inhibitory potencies. Immunocytochemical and co-immunoprecipitation studies demonstrated the in vivo interaction between the two PLD isozymes and actin in cells. Taken together, these results suggest that the regulation of PLD by cytoskeletal proteins, ␤-actin and ␣-actinin, and ARF1 may play an important role in cytoskeleton-related PLD functions. Mammalian phospholipase D (PLD)1 hydrolyzes phosphatidylcholine (PC) to generate phosphatidic acid and choline in response to a variety of signals, which can include hormones, neurotransmitters, and growth factors (1). phosphatidic acid itself has been shown to be an intracellular lipid second messenger and to be involved in multiple physiological events such as the promotion of mitogenesis, stimulation of respiratory bursts, secretory processes, actin cytoskeletal reorganization, and the activation of Raf-1 kinase and phosphatidylinositol 4-phosphate (PtdIns4P) 5-kinase isoforms in a large number of cells. These relationships suggest that agonist-induced PLD activation may play roles in multiple signaling events (2-7). The mammalian PLD isozymes identified thus far, PLD1 and PLD2, share a sequence homology of ϳ50%, but they have very different regulatory properties. PLD1 has low basal activity in the presence of phosphatidylinositol-4,5-bisphosphate (PIP 2 ) and can be activated by several cytosolic factors including protein kinase C ␣ and small GTP-binding proteins such as Rho A, Rac-1, ARF1, RalA, and CDC42 (8 -15). PLD2 also depends on PIP 2 but has a higher basal activity than PLD1 (16), and it has been proposed that PLD2 may be closely associated with different cellular inhibitors. Alth...

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Stimulation of actin stress fibre formation mediated by activation of phospholipase D

Cited by 219 publications

References 37 publications

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Increased concentrations of phosphatidate, diacylglycerol and ceramide in ras- and tyrosine kinase (fps)-transformed fibroblasts

Actin Directly Interacts with Phospholipase D, Inhibiting Its Activity

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