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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Enzymatic characterization of phospholipase D of protozoan Tetrahymena cells.
TL;DR: The existence of evolutionally related PLD activity in the unicellular eukaryotic protozoan Tetrahymena was demonstrated, and it was found to be significantly and transiently elevated in the early logarithmic phase, indicating its possible role in the development of TetrahYmena.
Journal ArticleDOI
Integrated Analysis of Transcriptomic and Proteomics Data Reveals the Induction Effects of Rotenoid Biosynthesis of Mirabilis himalaica Caused by UV-B Radiation
Li Gu,Weilie Zheng,Mingjie Li,Hong Quan,Wang Jianming,Fengji Wang,Wei Huang,Yunfang Wu,Xiaozhong Lan,Zhongyi Zhang +9 more
TL;DR: RNA sequencing and iTRAQ techniques were used to investigate the critical molecular “events” of rotenoid biosynthesis responding to UV-B radiation, and showed that the plant hormone signal transduction and phosphatidylinositol signaling system might be the key metabolic strategy to improve the biosynthesis ofrotenoid in M. himalaica.
Journal ArticleDOI
Mammalian PITPs at the Golgi and ER-Golgi Membrane Contact Sites:
Shamshad Cockcroft,Sima Lev +1 more
TL;DR: The function of mammalian PITPs at the Golgi and ER-Golgi membrane contact sites (MCS) is discussed and DAG (Diacylglycerol) is highlighted as a central hub of PITPs functions and PITPs-associated phospho-signaling network at the ER-golgi interface is described.
Journal ArticleDOI
The role of phospholipase D in Glut-4 translocation
Ping Huang,Michael A. Frohman +1 more
TL;DR: Current investigation is centered on Phospholipase D promotion of Glut‐4‐containing membrane vesicle trafficking and vesicles fusion into the plasma membrane, in part through activation of atypical protein kinase C isoforms.
Journal ArticleDOI
Protein Kinase C-epsilon in Membrane Delivery during Phagocytosis
TL;DR: A model for PKC-ε mediated vesicle formation for exocytosis during phagocytotic that may be applicable to other processes that require directed membrane delivery and fusion is proposed.
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