Phospholipase D Stimulates Release of Nascent Secretory Vesicles from the trans-Golgi Network
Ye-Guang Chen,Anirban Siddhanta,Cary D. Austin,Scott M. Hammond,Tsung Chang Sung,Michael A. Frohman,Andrew J. Morris,Dennis Shields +7 more
TLDR
It is demonstrated that immunoaffinity-purified human PLD1 stimulated nascent secretory vesicle budding from the TGN and ARF-1 stimulated endogenous PLD activity in Golgi membranes approximately threefold and this activation correlated with its enhancement of vesicles budding.Abstract:
Phospholipase D (PLD) is a phospholipid hydrolyzing enzyme whose activation has been implicated in mediating signal transduction pathways, cell growth, and membrane trafficking in mammalian cells. Several laboratories have demonstrated that small GTP-binding proteins including ADP-ribosylation factor (ARF) can stimulate PLD activity in vitro and an ARF-activated PLD activity has been found in Golgi membranes. Since ARF-1 has also been shown to enhance release of nascent secretory vesicles from the TGN of endocrine cells, we hypothesized that this reaction occurred via PLD activation. Using a permeabilized cell system derived from growth hormone and prolactin-secreting pituitary GH3 cells, we demonstrate that immunoaffinity-purified human PLD1 stimulated nascent secretory vesicle budding from the TGN approximately twofold. In contrast, a similarly purified but enzymatically inactive mutant form of PLD1, designated Lys898Arg, had no effect on vesicle budding when added to the permeabilized cells. The release of nascent secretory vesicles from the TGN was sensitive to 1% 1-butanol, a concentration that inhibited PLD-catalyzed formation of phosphatidic acid. Furthermore, ARF-1 stimulated endogenous PLD activity in Golgi membranes approximately threefold and this activation correlated with its enhancement of vesicle budding. Our results suggest that ARF regulation of PLD activity plays an important role in the release of nascent secretory vesicles from the TGN.read more
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OtherDOI
Phospholipid‐Derived Second Messengers
TL;DR: The sections in this article are: Inositol Phospholipid Hydrolysis, Functional Significance, and Role of Phosphatidylinositol 3-Kinase in Cell Function.
Journal ArticleDOI
Lipid-Mediated Regulation of Extrinsic Membrane Protein Activities
Jennifer Kitchen,Elliott Crooke +1 more
TL;DR: It is increasingly apparent that lipids function not only in the membranous compartmentalization of cell components, but also in the regulation of activities of soluble proteins involved in key cellular events.
Dissertation
Régulation des la voie mTOR par la phospholipase D dans le muscle squelettique : implication dans le contrôle de la différenciation myogénique et de la taille des myocytes
TL;DR: In this paper, the effect of the phospholipase D (PLD) on the activations of mTORC1 and mTORc2 was investigated, and it was shown that the PLD is susceptible to playing a role myogenique and anti-atrophique in the controle of the myoblastes.
Dissertation
Characterisation of PLD activity in real-time
TL;DR: Findings will facilitate future development of a live real-time in vivo PLD assay and help clarify the relative rate of PLD activation in response to small G-protein activators and other co-factors in real- time.
Posted ContentDOI
Phosphatidic acid produced by phospholipase D is required for hyphal cell-cell fusion and fungal-plant symbiosis
Berit Hassing,Carla J. Eaton,David J. Winter,Kimberly A. Green,Ulrike Brandt,Matthew S. Savoian,Carl H. Mesarich,Andre Fleissner,Barry Scott +8 more
TL;DR: It is found that E. festucae PldB and the N. crassa ortholog, PLA-7, are required for polarized growth, cell fusion and ascospore development, whereas PldA/PLA-8 are dispensable for these functions.
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