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Phospholipase D1: a key factor for the exocytotic machinery in neuroendocrine cells
TLDR
The activation of an ADP ribosylation factor‐regulated PLD at the plasma membrane of chromaffin cells undergoing secretagogue‐stimulated exocytosis is described and it is shown here that the isoform involved is PLD1b, and, using a real‐time assay for individual cells, that PLD activation and exocyTosis are closely correlated.
Phospholipase D1 Production of Phosphatidic Acid at the Plasma Membrane Promotes Exocytosis of Large Dense-core Granules at a Late Stage*
TLDR
It is demonstrated that phospholipase D1 is activated in secretagogue-stimulated cells and that it produces PA at the plasma membrane at the secretory granule docking sites and proposed that the underlying mechanism is related to the ability of PA to alter membrane curvature and promote hemi-fusion.
Calcium-regulated exocytosis of dense-core vesicles requires the activation of ADP-ribosylation factor (ARF)6 by ARF nucleotide binding site opener at the plasma membrane
TLDR
The results provide the first direct evidence that ARF6 plays a role in calcium-regulated exocytosis in neuroendocrine cells, and suggest that ARf6-stimulated PLD1 activation at the plasma membrane and consequent changes in membrane phospholipid composition are critical for formation of the exocyTotic fusion pore.
Regulated Exocytosis in Chromaffin Cells
TLDR
It is found that stimulation of intact chromaffin cells or direct elevation of cytosolic calcium in permeabilized cells triggered the rapid translocation of ARF6 from secretory granules to the plasma membrane and the concomitant activation of PLD in the plasma membranes.
Regulated Exocytosis in Chromaffin Cells
TLDR
It is found that ARF6 is specifically associated with the membrane of purified secretory chromaffin granules, and a synthetic myristoylated peptide corresponding to the N-terminal domain of ARf6 strongly inhibited calcium-evoked secretion in streptolysin-O-permeabilized Chromaffin cells.
Role of phosphoinositide signaling in the control of insulin exocytosis.
TLDR
The data indicate that the production of PI(4,5)P(2) is necessary for proper control of beta-cell secretion and suggest that at least part of the effect of PI on insulin exocytosis could be exerted through the activation of phospholipase D1, Ca(2+)-dependent activator protein for secretion 1, and Munc18-interacting protein 1.
The Small GTPase RalA Controls Exocytosis of Large Dense Core Secretory Granules by Interacting with ARF6-dependent Phospholipase D1*
TLDR
Evidence is provided that RalA is a positive regulator of calcium-evoked exocytosis of large dense core secretory granules and suggest that stimulation of PLD1 and consequent changes in plasma membrane phospholipid composition is the major function RAlA undertakes in calcium-regulated exocyTosis.
Regulation of phospholipase D1 subcellular cycling through coordination of multiple membrane association motifs
TLDR
It is proposed that PLD1 localization and function involves regulated and continual cycling through a succession of subcellular sites, mediated by successive combinations of membrane association interactions.
Regulated exocytosis in neuroendocrine cells: a role for subplasmalemmal Cdc42/N-WASP-induced actin filaments.
TLDR
The results demonstrate for the first time that secretagogue-evoked stimulation induces the sequential ordering of Cdc42, N-WASP, and Arp2/3 at the interface between granules and the plasma membrane, thereby providing an actin structure that makes the exocytotic machinery more efficient.
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