Phospholipase D: a Downstream Effector of ARF in Granulocytes

Cockcroft, Shamshad; Thomas, Geraint M. H.; Fensome, Amanda; Geny, Blandine; Cunningham, Emer; Gout, Ivan; Hiles, Ian D.; Totty, Nicholas F.; Truong, Oanh; Hsuan, J. Justin

doi:10.1126/science.8290961

Cited by 635 publications

(403 citation statements)

References 29 publications

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“…In this case, one would have to assume that this peptide, which is only 15 amino acid residues long, suffices to mediate the recruitment of these coat proteins to the TGN membrane. An alternative interpretation, which we favour, is that the stimulation of biogenesis of TGN-derived secretory vesicles by the N-myristoylated ARF1 peptide reflected the activation of phospholipase D. Phospholipase D appears to be present on Golgi membranes [29], is stimulated by ARF via ARF's myristoylated amino-terminal domain [30][31][32], and this stimulation is inhibited by brefeldin A [29]. Perhaps the Nmyristoylated ARF1 peptide was more potent in eliciting a phospholipase D activation relevant to TGN-derived secretory vesicle biogenesis than the N-myristoylated ARF4 peptide [33].…”

Section: Discussionmentioning

confidence: 88%

A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

Barr

Huttner

1996

FEBS Letters

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A synthetic N-myristoylated peptide corresponding to the amino-terminal domain of ADP-ribosylation factor 1 (ARF1) markedly increases, in a cell-free system using post-nuclear supernatant from PC12 cells, the biogenesis of constitutive secretory vesicles and immature secretory granules from the trans-Goigi network (TGN). The related N-myristoylated ARF4 peptide only weakly stimulates, and the non-myristoylated ARF1 and ARF4 peptides inhibit, the biogenesis of these secretory vesicles. In a modified cell-free system using TGN membranes, eoatomer-depleted cytosol supports the biogenesis of TGNderived secretory vesicles to the same extent as control cytosol. These results suggest a role for ARF1, but not the COP I coat, in secretory vesicle biogenesis from the TGN, possibly via the activation of phospholipase D. [10,11], the biogenesis of both CSVs and ISGs, collectively referred to as TGN-derived secretory vesicles, is inhibited by brefeldin A. If one extrapolates from the observations on the formation of cis-Golgi-derived vesicles to the biogenesis of TGN-derived secretory vesicles, the inhibition by brefeldin A would be indicative of an involvement of ARF in the latter process [12]. In the present study, we have examined a possible role of ARF in the biogenesis of TGN-derived secretory vesicles. In addition, we have addressed the related question of whether or not coatomer is required for the biogenesis of these vesicles. Materials and methods

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Section: Discussionmentioning

confidence: 88%

A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

Barr

Huttner

1996

FEBS Letters

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“…They are essential molecules for coated vesicle formation in the Golgi complex (4,5) and have also been implicated in vesicle transport between endoplasmic reticulum and Golgi (6,7) and in nuclear vesicle fusion (8). More recently, ARFs have been shown to activate phospholipase D (9,10).…”

mentioning

confidence: 99%

Arfaptin 1, a Putative Cytosolic Target Protein of ADP-ribosylation Factor, Is Recruited to Golgi Membranes

Kanoh

Williger

Exton

1997

Journal of Biological Chemistry

112

101

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ADP-ribosylation factors (ARFs) have been implicated in vesicle transport in the Golgi complex. Employing yeast two-hybrid screening of an HL60 cDNA library using a constitutively active mutant of ARF3 (ARF3⅐Q71L), as a probe, we have identified a cDNA encoding a novel protein with a calculated molecular mass of 38.6 kDa, which we have named arfaptin 1. The mRNA of arfaptin 1 was ubiquitously expressed, and recombinant arfaptin 1 bound preferentially to class I ARFs, especially ARF1, but only in the GTP-bound form. The interactions were independent of myristoylation of ARF. Arfaptin 1 in cytosol was recruited to Golgi membranes by ARF in a guanosine 5 -O-(3-thiotriphosphate)-dependent and brefeldin A-sensitive manner. When expressed in COS cells, arfaptin 1 was localized to the Golgi complex. The yeast two-hybrid system yielded another clone, which encoded a putative protein, which we have named arfaptin 2. This consisted of the same number of amino acids as arfaptin 1 and was 60% identical to it. Arfaptin 2 was also ubiquitously expressed and bound to the GTP-, but not GDP-liganded form of class I ARFs, especially ARF1. These results suggest that arfaptins 1 and 2 may be direct target proteins of class 1 ARFs. Arfaptin 1 may be involved in Golgi function along with ARF1.

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“…We have previously reported that bombesin-stimulated PLD activity was also regulated by guanine-nucleotides, though whether a G-protein other than Gq was involved was not determined [14]. However there is evidence that the small molecular weight G-proteins ARF [6,7] and rho [15] can regulate activity. Experiments were thus performed to investigate whether a short agonist exposure could affect the stimulation of PLD activity through G-protein activation alone.…”

Section: ~ Results and Discussionmentioning

confidence: 99%

“…It remains incompletely defined as to how an occupied cell surface receptor stimulates PLD activity, but activation has been proposed to be downstream of protein kinase C activity, tyrosine kinase activity or changes in calcium concentration, a role for the small molecular weight G-protein ARF in directly regulating PLD has also been proposed [6,7]. Bombesin-stimulated PLD activity in Swiss 3T3 cells as deter-*Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Heterologous desensitization of bombesin‐ and vasopressin‐stimulated phospholipase D activity in Swiss 3T3 fibroblasts

Briscoe

Wakelam

1995

FEBS Letters

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Bombesin-and vasopressin-stimulated phospholipase D (PLD) activities are rapidly desensitized in 3T3 cells, in addition both agonists are subject to heterologous desensitization. Binding studies showed that homologous desensitization was partly a result of loss of cell surface receptors, whilst heterologous desensitization was independent of receptor changes. Pretreatment with either agonist reduced subsequent GTPyS-stimulated PLD activity by 50% whereas a pretreatment with GTPyS did not attenuate the response, suggesting that the G-protein or downstream effector systems were affected by receptor activation resulting in desensitization. The desensitization of receptor-stimulated PLD activation provides support for the phospholipase functioning in a key signalling pathway.

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Phospholipase D: a Downstream Effector of ARF in Granulocytes

Cited by 635 publications

References 29 publications

A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

Arfaptin 1, a Putative Cytosolic Target Protein of ADP-ribosylation Factor, Is Recruited to Golgi Membranes

Heterologous desensitization of bombesin‐ and vasopressin‐stimulated phospholipase D activity in Swiss 3T3 fibroblasts

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