New Developments in Phospholipase D

Exton, John H.

doi:10.1074/jbc.272.25.15579

Cited by 295 publications

(282 citation statements)

References 78 publications

(112 reference statements)

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“…The linkage of PKC to the PLD signal transduction pathway may depend on the tissue and the stage of development studied (Briscoe et al, 1995;Exton, 1997;Klein et al, 1997;Schmidt et al, 1996). Additionally, it has been reported that PKC activation of PLD may occur by ATP independent mechanism (Conricode et al, 1992;Singer et al, 1996), and this mechanism would not be inhibited by the bisindolemalemide family of PKC inhibitors since their action is due to a competitive inhibition of the ATP binding site (Gordge & Ryves, 1994).…”

Section: Discussionmentioning

confidence: 99%

“…The regulation of PLD can have important consequences because it generates two di erent second messengers (DAG and PA), each with its own signalling potential (English, 1996;Exton, 1997;Hodgkin et al, 1998). In particular, DAGs derived from PI or PC appear to di er in their ability to induce the translocation of selective PKC isoforms and the time scale of the PKC activation (Ha & Exton, 1993).…”

Section: Discussionmentioning

confidence: 99%

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Activation of phospholipase D by metabotropic glutamate receptor agonists in rat cerebrocortical synaptosomes

Shinomura

Río

Breen

et al. 2000

British J Pharmacology

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1 The pharmacological pro®le of metabotropic glutamate receptor (mGluR) activation of phospholipase D (PLD), and the associated signalling pathways, were examined in rat cerebrocortical synaptosomes. The assay was conducted using a transphosphatidylation reaction in synaptosomes which were pre-labelled with either [ 3 H]-arachidonic acid or [ 32 P]-orthophosphate. 2 The mGluR agonists (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid (1S,3R-ACPD) and (RS)-3,5-dihydroxyphenylglycine (DHPG), both activated PLD, while phorbol 12,13-dibutyrate (PDBu) treatment caused receptor-independent activation of PLD and had an additive e ect on 1S,3R-ACPD induced PLD activity. 3 A protein kinase C (PKC) inhibitor, GF109203X, failed to antagonize mGluR receptor-coupled PLD activity. We could not detect any increase in the products of PI (phosphoinositide)-speci®c phospholipase C (PI-PLC), inositol(1,4,5)trisphosphate or diacylglycerol, by 1S, 3R-ACPD at 15 s. However, diacylglycerol increased monophasically in response to mGluR agonists and remained elevated for at least 15 min. Phosphatidic acid phosphohydrolase (PAP) activity, which converts PA to DAG, was present in the synaptosomes. 4 These data suggest that, in rat cerebrocortical synaptosomes, the 1S,3R-ACPD-sensitive mGluR is coupled to PLD through a mechanism that is independent of both PKC and PI-PLC.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Activation of phospholipase D by metabotropic glutamate receptor agonists in rat cerebrocortical synaptosomes

Shinomura

Río

Breen

et al. 2000

British J Pharmacology

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“…In contrast to negative regulation of Rac, sequestration of RalBP1 by Ral-GTP possibly elevates basal levels of active Rac. PLD1 may couple to NF-B and cyclin D1 through production of second messenger phosphatidic acid, lysophosphatidic acid, or diacylglycerol (13). To examine the effector dependency of Ral activation of NF-B and cyclin D1, we tested the activity of Ral variants that uncouple association of Ral with RalBP1 versus PLD1.…”

Section: Resultsmentioning

confidence: 99%

“…However, activation of Ral cooperates with ADP ribosylation factor GTPases to activate PLD1, perhaps by contributing to the formation of a PLD1 activation complex (28,35). There is some evidence that active PLD1 can contribute to proliferation (13). For example, transfected PLD1 can contribute to oncogenic transformation of fibroblasts overexpressing epidermal growth factor (EGF) receptors (34).…”

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confidence: 99%

Ral GTPases Contribute to Regulation of Cyclin D1 through Activation of NF-κB

Henry

Moskalenko

Kaur

et al. 2000

Molecular and Cellular Biology

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“…It has been demonstrated recently that PKCε, due to the lack of Ca 2+ binding, interacts with low specificity with PS and DAG, which implies the presence of other physiological activators for this form [39]. For example, it is well established that PLD activation induces an increase of phosphatidic acid in biological membranes [27] and this could be a way of activating PKCε. As it was demonstrated previously [23] the PKCε-C2 domain has an important affinity for phosphatidic acid vesicles although the secondary structure of the domain did not change upon lipid binding, in contrast with PKCα-C2 domain that underwent significant changes ( [23] and this work).…”

Section: Comparison Of C2 From Pkcα and C2 From Pkcεmentioning

confidence: 99%

Structural Characterization of the C2 Domains of Classical Isozymes of Protein Kinase C and Novel Protein Kinase Cε by using Infrared Spectroscopy

Corbalán-Garcı́a

Garcı́a-Garcı́a

Sánchez-Carrillo

et al. 2003

Journal of Spectroscopy

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Abstract. The amide I regions in the original infrared spectra of PKCα-C2 in the Ca 2+ -free and Ca 2+ -bound states are both consistent with a predominantly β-sheet secondary structure. Spectroscopic studies of the thermal denaturation revealed that for the PKCα-C2 domain alone the secondary structure abruptly changed at 50 • C. While in the presence of Ca 2+ , the thermal stability of the protein increased considerably. Phosphatidic acid binding to the PKCα-C2 domain was characterized, and the lipid-protein binding becoming Ca 2+ -independent when 100 mol% phosphatidic acid vesicles was used. The effect of lipid binding on secondary structure and thermal stability was also studied. In addition, the secondary structure of the C2 domain from the novel PKCε was also determined by IR spectroscopy and β-sheet was seen to be the major structural component. Spectroscopic studies of the thermal denaturation in D2O showed a broadening in the amide I band starting at 45 • C. Phosphatidic acid containing vesicles were used to characterize the effect of lipid binding on the secondary structure. It was observed through thermal stability experiments that the secondary structure did not change upon lipid binding and the protein stability was very high with no significant changes occurring in the secondary structure after heating.

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New Developments in Phospholipase D

Cited by 295 publications

References 78 publications

Activation of phospholipase D by metabotropic glutamate receptor agonists in rat cerebrocortical synaptosomes

Activation of phospholipase D by metabotropic glutamate receptor agonists in rat cerebrocortical synaptosomes

Ral GTPases Contribute to Regulation of Cyclin D1 through Activation of NF-κB

Structural Characterization of the C2 Domains of Classical Isozymes of Protein Kinase C and Novel Protein Kinase Cε by using Infrared Spectroscopy

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