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Phospholipase D and membrane traffic - Potential roles in regulated exocytosis, membrane delivery and vesicle budding

Jones, D; Morgan, C; Cockcroft, S; (1999) Phospholipase D and membrane traffic - Potential roles in regulated exocytosis, membrane delivery and vesicle budding. BBA-MOL CELL BIOL L , 1439 (2) 229 - 244.

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Abstract

It is now well-established that phospholipase D is transiently stimulated upon activation by G-protein-coupled and receptor tyrosine kinase cell surface receptors in mammalian cells. Over the last 5 years, a tremendous effort has gone to identify the major intracellular regulators of mammalian phospholipase D and to the cloning of two mammalian phospholipase D enzymes (phospholipase D1 and D2). In this chapter, we review the physiological function of mammalian phospholipase D1 that is synergistically stimulated by ADP ribosylation factor, Rho and protein kinase Ca. We discuss the function of this enzyme in membrane traffic, emphasising the possible integrated relationships between consumption of vesicles in regulated exocytosis, membrane delivery and constitutive membrane traffic. (C) 1999 Elsevier Science B.V, All rights reserved.

Type: Article
Title: Phospholipase D and membrane traffic - Potential roles in regulated exocytosis, membrane delivery and vesicle budding
Keywords: exocytosis, membrane trafficking, vesicle budding, ADP-RIBOSYLATION-FACTOR, PHOSPHATIDYLINOSITOL TRANSFER PROTEIN, GUANINE-NUCLEOTIDE-EXCHANGE, GTP-BINDING PROTEINS, STIMULATED HUMAN-NEUTROPHILS, NASCENT SECRETORY VESICLES, HL-60 CELLS, MAST-CELLS, KINASE-C, PLASMA-MEMBRANE
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Neuro, Physiology and Pharmacology
URI: http://discovery.ucl.ac.uk/id/eprint/119620
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