ARF signaling: A potential role for phospholipase D in membrane traffic

Kahn, Richard; Yucel, Jennifer K.; Malhotra, Vivek

doi:10.1016/0092-8674(93)90314-g

Cited by 163 publications

(89 citation statements)

References 17 publications

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“…1B) suggests that the enzyme may play a special role in brain and mature testis. Thus PA-PLA1 might attenuate agonistgenerated PA signals such as those mentioned earlier (2)(3)(4)(5) or signals that affect vesicle transport processes (28). In this light, our observation that PA-PLA1 preferentially hydrolyzes diunsaturated PA (Fig.…”

Section: Resultsmentioning

confidence: 55%

Identification of a phosphatidic acid-preferring phospholipase A1 from bovine brain and testis.

Higgs

Glomset²

1994

Proc. Natl. Acad. Sci. U.S.A.

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Recent experiments in several laboratories have provided evidence that phosphatidic acid functions in cell signaling. However, the mechaninsm that regulate cellular phosphatidic acid levels remain obscure. Here we describe a soluble phospholipase Al from bovine testis that preferentially hydrolyzes phosphatidic acid when assayed in Triton X-100 micelles. Moreover, the enzyme hydrolyzes phosphatidic acid molecular species containing two unsaturated fatty acids in preference to those containing a combination of saturated and unsaturated fatty acyl groups. Under certain conditions, the enzyme also displays lysophospholipase activity toward lysophosphatidic acid. The phospholipase Al is not likely to be a lysosomal enzyme because its optimum pH is 7.5-8.5. Furthermore, it is probably not a general lipid metabolic enzyme because high levels ofactiv are found in mature testis and brain but no measurable activity is seen in liver, spleen, or heart. The fact that the activity of the phospholipase A1 in mature bovine testis is >10-fold higher than that in newborn calf testis raises the possibility that the enzyme may play a regulatory role in spermatogenesis or sperm function.

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Section: Resultsmentioning

confidence: 55%

Identification of a phosphatidic acid-preferring phospholipase A1 from bovine brain and testis.

Higgs

Glomset²

1994

Proc. Natl. Acad. Sci. U.S.A.

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“…ARFs appear ideally suited to regulate this switch between tubular fusion with like-membranes and production of vesicles destined for the next compartment. Additional functions for members of this multigene family have been identified (Brown et al, 1993;Kahn et al, 1993), and further biochemical and cell biological characterization of individual ARFs will more clearly define their putative multi-functional roles in intracellular processes.…”

Section: Function Of Arfs In the Golgi And Other Endomembrane Systemsmentioning

confidence: 99%

Cytosolic ARFs are required for vesicle formation but not for cell-free intra-Golgi transport: evidence for coated vesicle-independent transport.

Taylor

Kanstein

Weidman

et al. 1994

MBoC

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We investigated the role of ADP-ribosylation factors (ARFs) in Golgi function using biochemical and morphological cell-free assays. An ARF-free cytosol produced from soluble Chinese hamster ovary (CHO) extracts supports intra-Golgi transport by a mechanism that is biochemically indistinguishable from control transport reactions: ARF-free transport reactions are NSF-dependent, remain sensitive to the donor Golgi-specific inhibitor ilimaquinone, and exhibit kinetics that are identical to that of control reactions containing ARFs. In contrast, ARF-free cytosol does not support the formation of coated vesicles on Golgi cistemae. However, vesicle formation is reconstituted upon the addition of ARF1. These data suggest that neither soluble ARFs nor coated vesicle formation are essential for transport. We conclude that cell-free intra-Golgi transport proceeds via a coated vesicle-independent mechanism regardless of vesicle formation on Golgi cistemae.

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“…Brefeldin A causes dissociation of ARF and b-COP from Golgi membranes in vivo and in vitro, and these effects occur before the Golgi membranes are redistributed to the endoplasmic reticulum . The inhibition of ARF activation and association with Golgi membranes induced by brefeldin A are postulated to inhibit p-COP binding and induce changes in Golgi morphology [5,[9][10][11][12].…”

mentioning

confidence: 99%

Effects of Brefeldin A on Phosphatidylcholine Phospholipase D and Inositolphospholipid Metabolism in HL‐60 Cells

Guillemain

Exton

1997

European Journal of Biochemistry

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The involvement of the small GTP-binding protein ADP-ribosylation factor (ARF) in guanosine 5'- [y-thio] triphosphate (GTP[S])-dependent activation of phospholipase D (PLD) in HL-60 cells has been well established in vitro.In this study, we tested the effect of brefeldin A, which prevents ARF activation by inhibiting guanine-nucleotide-exchange activity, on PLD stimulation by receptor agonists (formylMet-Leu-Phe and ATP) and by the phorbol ester phorbol 12-myristate 13-acetate (PMA) in differentiated HL-60 cells. However, brefeldin A did not affect the activation of PLD at a time (1 h) when it eliminated the activity of the trans-Golgi enzyme galactosyltransferase. It also did not inhibit PLD activity in Golgienriched membranes treated with GTP[S] with or without ARF in vitro. However, longer times of brefeldin A treatment (> 6 h), progressively and completely inhibited the activation of PLD by formyl-MetLeu-Phe and partly inhibited (~5 0 % ) the activation by PMA. In contrast, long-term brefeldin A treatment did not inhibit the effect of GTP[S] on PLD in permeabilized HL-60 cells. Long-term brefeldin A treatment completely inhibited inositol phosphate production in response to formyl-Met-Leu-Phe and ATP, indicating that it affected inositolphospholipid-specific phospholipase C activity. These data indicate that the rapid inhibitory effect of brefeldin A on Golgi function is not associated with inhibition of receptormediated or PMA-mediated PLD activation in HL-60 cells. However, longer-term effects, presumably arising from the disruption of the Golgi, lead to a total inhibition of agonist activation of PLD and inositolphospholipid-specific phospholipase C. In summary, these results do not support a role for brefeldin-A-sensitive ARF in agonist regulation of PLD in HL-60 cells.Keywords: phospholipase D ; ADP-ribosylation factor; brefeldin A; inositolphospholipid; Golgi.Brefeldin A is a fungal metabolite, initially reported to inhibit protein secretion [l]. It inhibits vesicular transport in the Golgi complex and causes a rapid resorption of most of the Golgi membrane into the endoplasmic reticulum [2] and association of Golgi enzymes with the endoplasmic reticulum, thereby eliminating the Golgi complex as a morphologically distinct organelle [3]. Morphological changes in the Golgi and redistribution of Golgi markers are observed within minutes of addition of brefeldin A. Upon removal of brefeldin A, the morphology of the Golgi is rapidly restored, and normal protein transport and sorting resumes.The earliest detectable event in the action of brefeldin A is prevention of the GTP-dependent interaction with Golgi membranes of ADP-ribosylation factor (ARF), a small GTP-binding protein [4]. A protein that catalyzes the exchange of guanine nucleotide on ARF has been identified in Golgi preparations and shown to be specifically inhibited by brefeldin A [5, 61. Since ARF binding on Golgi membranes is required for the association of the p-coatamer protein (/I-COP), a component of coatomers, PLD activation by guanosine 5...

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ARF signaling: A potential role for phospholipase D in membrane traffic

Cited by 163 publications

References 17 publications

Identification of a phosphatidic acid-preferring phospholipase A1 from bovine brain and testis.

Identification of a phosphatidic acid-preferring phospholipase A1 from bovine brain and testis.

Cytosolic ARFs are required for vesicle formation but not for cell-free intra-Golgi transport: evidence for coated vesicle-independent transport.

Effects of Brefeldin A on Phosphatidylcholine Phospholipase D and Inositolphospholipid Metabolism in HL‐60 Cells

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