Phospholipase D

2004 ◽  
Vol 82 (1) ◽  
pp. 225-253 ◽  
Author(s):  
Mark McDermott ◽  
Michael J.O Wakelam ◽  
Andrew J Morris
Keyword(s):  
Phosphatidic Acid ◽  
Membrane Transport ◽  
Phospholipase D ◽  
Binding Proteins ◽  
Acid Product ◽  
Diverse Range ◽  
Phosphodiester Bond ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Intracellular Membrane Transport

Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals. Although enzymes with broader selectivity are found in some of the lower organisms, the plant, yeast, and mammalian enzymes are selective for phosphatidylcholine. The two mammalian phospholipase D isoforms are regulated by protein kinases and GTP binding proteins of the ADP-ribosylation and Rho families. Mammalian and yeast phospholipases D are also potently stimulated by phosphatidylinositol 4,5-bisphosphate. This review discusses the identification, characterization, structure, and regulation of phospholipase D. Genetic and pharmacological approaches implicate phospholipase D in a diverse range of cellular processes that include receptor signaling, control of intracellular membrane transport, and reorganization of the actin cytoskeleton. Most ideas about phospholipase D function consider that the phosphatidic acid product is an intracellular lipid messenger. Candidate targets for phospholipase-D-generated phosphatidic acid include phosphatidylinositol 4-phosphate 5-kinases and the raf protein kinase. Phosphatidic acid can also be converted to two other lipid mediators, diacylglycerol and lyso phosphatidic acid. Coordinated activation of these phospholipase-D-dependent pathways likely accounts for the pleitropic roles for these enzymes in many aspects of cell regulation.Key words: phospholipase D, phosphatidic acid, GTP-binding proteins, membrane transport, cytoskeletal regulation.

Small GTPase-regulated phospholipase D in granulocytes

1996 ◽  
Vol 74 (4) ◽  
pp. 459-467 ◽  
Author(s):  
Martin G. Houle ◽  
Sylvain Bourgoin
Keyword(s):  
Molecular Weight ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Tyrosine Kinases ◽  
Binding Proteins ◽  
Active Role ◽  
Small Gtpase ◽  
Low Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding

This review examines the functional role of phospholipase D in the neutrophil. Phospholipase D is emerging as an important component in the signal transduction pathways leading to granulocyte activation. Through the second messenger it produces, phosphatidic acid, phospholipase D plays an active role in the regulation of granulocyte NADPH oxidase activation and granular secretion. Many factors from both the cytosol and the membrane are necessary for maximal phospholipase D activation. This paper will focus on the regulation of phospholipase D by low molecular weight GTP-binding proteins, tyrosine kinases, and protein kinase C.Key words: phospholipase D, low molecular weight GTP-binding proteins, tyrosine kinases, protein kinase C, granulocytes.

scholarly journals Regulation of Phospholipase D(PLD) Activation and Small GTP-Binding Proteins.

MEMBRANE ◽  
1996 ◽  
Vol 21 (3) ◽  
pp. 177-183
Author(s):  
Kenji Ohguchi ◽  
Yoshinori Nozawa
Keyword(s):  
Phospholipase D ◽  
Binding Proteins ◽  
Gtp Binding Proteins ◽  
Gtp Binding

scholarly journals ROLE OF RHO FAMILY GTP-BINDING PROTEINS IN IgE RECEPTOR-MEDIATED PHOSPHOLIPASE D ACTIVATION IN MAST CELLS

1998 ◽  
Vol 19 (1) ◽  
pp. 53-63
Author(s):  
KATSUHIRO OJIO ◽  
YOSHIKO BANNO ◽  
KAZUKI HAYAKAWA ◽  
YATSUJI ITO ◽  
NAOKI KATO ◽  
...  
Keyword(s):  
Mast Cells ◽  
Phospholipase D ◽  
Binding Proteins ◽  
Ige Receptor ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Rho Family

scholarly journals Rabs and EHDs: alternate modes for traffic control

2011 ◽  
Vol 32 (1) ◽  
pp. 17-23 ◽  
Author(s):  
Jing Zhang ◽  
Naava Naslavsky ◽  
Steve Caplan
Keyword(s):  
Membrane Transport ◽  
Traffic Control ◽  
Binding Proteins ◽  
Endocytic Trafficking ◽  
Rab Proteins ◽  
Protein Families ◽  
Vesicle Budding ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Key Aspects

Endocytic trafficking is a highly organized process regulated by a network of proteins, including the Rab family of small GTP-binding proteins and the C-terminal EHDs (Eps15 homology-domain-containing proteins). Central roles for Rab proteins have been described in vesicle budding, delivery, tethering and fusion, whereas little is known about the functions of EHDs in membrane transport. Common effectors for these two protein families have been identified, and they facilitate regulation of sequential steps in transport. By comparing and contrasting key aspects in their modes of function, we shall promote a better understanding of how Rab proteins and EHDs regulate endocytic trafficking.

scholarly journals YsxC, a Putative GTP-Binding Protein Essential for Growth of Bacillus subtilis 168

2000 ◽  
Vol 182 (23) ◽  
pp. 6819-6823 ◽  
Author(s):  
Zoltán Prágai ◽  
Colin R. Harwood
Keyword(s):  
Bacillus Subtilis ◽  
Binding Proteins ◽  
Essential Gene ◽  
Binding Protein ◽  
Inducible Promoter ◽  
Gtp Binding Protein ◽  
Diverse Range ◽  
Gtp Binding Proteins ◽  
Bacillus Subtilis 168 ◽  
Gtp Binding

ABSTRACT YsxC is a member of a family of GTP-binding proteins carried by a diverse range of organisms from bacteria to yeasts, plants, and humans. To resolve the issue of whether ysxC of Bacillus subtilis is essential for growth, we attempted to construct mutants in which ysxC was either inactivated or placed under the control of an inducible promoter. Viable mutants were obtained only in the latter case, and these were inducer dependent, demonstrating unambiguously that ysxC is an essential gene.

Small GTP-binding Protein RalA Associates with Weibel-Palade Bodies in Endothelial Cells

1999 ◽  
Vol 82 (09) ◽  
pp. 1177-1181 ◽  
Author(s):  
Hubert de Leeuw ◽  
Pauline Wijers-Koster ◽  
Jan van Mourik ◽  
Jan Voorberg
Keyword(s):  
Endothelial Cells ◽  
Binding Proteins ◽  
Binding Protein ◽  
Control Release ◽  
Small Gtpase ◽  
Gtp Binding Protein ◽  
Two Dimensional Gel Electrophoresis ◽  
Gtp Binding Proteins ◽  
Dense Granules ◽  
Gtp Binding

SummaryIn endothelial cells von Willebrand factor (vWF) and P-selectin are stored in dense granules, so-called Weibel-Palade bodies. Upon stimulation of endothelial cells with a variety of agents including thrombin, these organelles fuse with the plasma membrane and release their content. Small GTP-binding proteins have been shown to control release from intracellular storage pools in a number of cells. In this study we have investigated whether small GTP-binding proteins are associated with Weibel-Palade bodies. We isolated Weibel-Palade bodies by centrifugation on two consecutive density gradients of Percoll. The dense fraction in which these subcellular organelles were highly enriched, was analysed by SDS-PAGE followed by GTP overlay. A distinct band with an apparent molecular weight of 28,000 was observed. Two-dimensional gel electrophoresis followed by GTP overlay revealed the presence of a single small GTP-binding protein with an isoelectric point of 7.1. A monoclonal antibody directed against RalA showed reactivity with the small GTP-binding protein present in subcellular fractions that contain Weibel-Palade bodies. The small GTPase RalA was previously identified on dense granules of platelets and on synaptic vesicles in nerve terminals. Our observations suggest that RalA serves a role in regulated exocytosis of Weibel-Palade bodies in endothelial cells.

Rap1b Association with the Platelet Cytoskeleton Occurs in the Absence of Glycoproteins IIb/IIIa

1998 ◽  
Vol 79 (04) ◽  
pp. 832-836 ◽  
Author(s):  
Thomas Fischer ◽  
Christina Duffy ◽  
Gilbert White
Keyword(s):  
Molecular Weight ◽  
Divalent Cation ◽  
Binding Proteins ◽  
Binding Protein ◽  
Platelet Membrane ◽  
Low Molecular Weight ◽  
Membrane Glycoproteins ◽  
Gtp Binding Protein ◽  
Gtp Binding Proteins ◽  
Gtp Binding

SummaryPlatelet membrane glycoproteins (GP) IIb/IIIa and rap1b, a 21 kDa GTP binding protein, associate with the triton-insoluble, activation-dependent platelet cytoskeleton with similar rates and divalent cation requirement. To examine the possibility that GPIIb/IIIa was required for rap1b association with the cytoskeleton, experiments were performed to determine if the two proteins were linked under various conditions. Chromatography of lysates from resting platelets on Sephacryl S-300 showed that GPIIb/IIIa and rap1b were well separated and distinct proteins. Immunoprecipitation of GPIIb/IIIa from lysates of resting platelets did not produce rap1b or other low molecular weight GTP binding proteins and immunoprecipitation of rap1b from lysates of resting platelets did not produce GPIIb/IIIa. Finally, rap1b was associated with the activation-dependent cytoskeleton of platelets from a patient with Glanzmann’s thrombasthenia who lacks surface expressed glycoproteins IIb and IIIa. Based on these findings, we conclude that no association between GPIIb/IIIa and rap1b is found in resting platelets and that rap1b association with the activation-dependent cytoskeleton is at least partly independent of GPIIb/IIIa.

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