Phospholipase D activation in fibroblast membranes by the α and β isoforms of protein kinase C

Conricode, Kevin M.; Smith, John K.; Burns, David J.; Exton, John H.

doi:10.1016/0014-5793(94)80490-7

Cited by 89 publications

(38 citation statements)

References 33 publications

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“…In later studies, PLD was shown to be tyrosine phosphorylated after immunoprecipitation of PLD and immunoblotting with a phosphotyrosine antibody (Gomez-Cambronero, 1995). Stimulation of the G Conricode et al (1992Conricode et al ( , 1994, Ohguchi et al (1996), Hammond et al (1997), Lee et al (1997b), Min et al (1998), Park et al (1998), Sung et al (1999b), Zhang et al (1999) Bowman et al (1993), Kwak et al (1995), Malcolm et al (1994), Brown et al (1995), Siddiqi et al (1995), Singer et al (1996), Hammond et al (1997), Sung et al (1997), Yamazaki et al (1999) Kim et al (1999a), Chen and Exton (2005) AA, amino acid; BARS, brefeldin A ADP-ribosylated substrate; RSK, ribosomal S6 kinase.…”

Section: B Tyrosine Phosphorylationmentioning

confidence: 99%

Phospholipase D Signaling Pathways and Phosphatidic Acid as Therapeutic Targets in Cancer

2014

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Section: B Tyrosine Phosphorylationmentioning

confidence: 99%

Phospholipase D Signaling Pathways and Phosphatidic Acid as Therapeutic Targets in Cancer

2014

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“…Data from overexpression studies and in vitro experiments with purified or recombinant protein indicate that it is the calcium-dependent cPKC isoenzymes (␣ and ␤) that are the primary PKC regulators of PLD in the cell (23)(24)(25)(26). Additionally, there are some data to suggest possible isoenzyme-specific differences between PKC␤I and PKC␤II.…”

Section: Fig 3 Translocation Of Gfp-pkc␤ii Requires Kinase Activitymentioning

confidence: 99%

Isoenzyme-specific Translocation of Protein Kinase C (PKC)βII and not PKCβI to a Juxtanuclear Subset of Recycling Endosomes

Becker

Hannun

2004

Journal of Biological Chemistry

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Elucidation of isoenzyme-specific functions of individual protein kinase C (PKC) isoenzymes has emerged as an important goal in the study of this family of kinases, but this task has been complicated by modest substrate specificity and high homology among the individual members of each PKC subfamily. The classical PKC␤I and PKC␤II isoenzymes provide a unique opportunity because they are the alternatively spliced products of the ␤ gene and are 100% identical except for the last 50 of 52 amino acids. In this study, it is shown that green fluorescent protein-tagged PKC␤II and not PKC␤I translocates to a recently described juxtanuclear site of localization for PKC␣ and PKC␤II isoenzymes that arises with sustained stimulation of PKC. Mechanistically, translocation of PKC␤II to the juxtanuclear region required kinase activity. PKC␤II, but not PKC␤I, was found to activate phospholipase D within this time frame. Inhibitors of phospholipase D (1-butanol and a dominant negative construct) prevented the translocation of PKC␤II to the juxtanuclear region but not to the plasma membrane, thus demonstrating a role for phospholipase D in the juxtanuclear translocation of PKC␤II. Taken together, these results define specific biochemical and cellular actions of PKC␤II when compared with PKC␤I.Members of the protein kinase C (PKC) 1 superfamily of lipiddependent serine-threonine kinases function as integral signaling intermediates in the transmission of numerous extracellular signals. PKC currently consists of 11 closely related isoenzymes that can be grouped into 3 subfamilies (classical, novel, and atypical) on the basis of lipid cofactor requirements and structural homology (1, 2). A major form of cellular regulation of PKC involves the dynamic redistribution or "translocation" of PKC isoenzymes from cytosol to the plasma membrane. Membrane translocation of PKC is regulated through receptor-coupled lipid hydrolases that act on phosphoinositides and phosphatidylcholine to generate diacylglycerol (DAG) lipid second messengers. The recruitment and activation of PKC at membranes also link activation of the enzyme to the proximity of membrane protein substrates (3).One of the major targets of PKC is phosphatidylcholinespecific phospholipase D (PC-PLD) (4). Activated PC-PLD hydrolyzes the phosphodiester bond of phosphatidylcholine to generate free choline and phosphatidic acid, which is converted to DAG through the actions of lipid phosphate phosphatases. DAG derived from phosphatidylcholine hydrolysis has been proposed to mediate the reciprocal regulation of PKC, but there are incomplete and conflicting data on this topic (5-7). One possible functional significance of PC-PLD-derived DAG arises from the sustained presence of DAG in the membrane for extended periods of time and in relatively high concentrations in comparison with DAG derived from phosphoinositide-specific PLC, and this phosphatidylcholine-derived DAG has been proposed to mediate long-term cellular processes that require sustained PKC activation (8).The implication of ...

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“…Further evidence in support of PKC comes from studies where down regulation of PKC abolished agonist-stimulated PLD activity [5] whilst overexpression of PKC a or /I1 isoforms upregulates both PMA-activated as well as receptor-activated PLD activity [68]. More recently it has been reported that direct addition of PKC isoforms /3 or a stimulated PLD activity in membranes [9]. From studies in permeabilized cells and other cell-free systems, it has emerged that PLD activity can be regulated by guanine nucleotides indicating a role for a putative GTP-binding protein [l&12].…”

Section: Introductionmentioning

confidence: 99%

ARF1‐regulated phospholipase D in human neutrophils is enhanced by PMA and MgATP

1994

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Human neutrophil PLD activity stimulated with GTP-y-S was reconstituted with recombinant ARFl in cytosol-depleted cells. PMApretreatment of intact cells greatly enhanced the subsequent reconstitution of the ARFl-regulated PLD activity. This enhancement was only observed provided that the intact cells were pretreated with PMA, suggesting the stable recruitment of a cytosolic component, presumably protein kinase C, to the membranes. rARFl-reconstituted PLD activity was not dependent on MgATP, but could be considerably enhanced by MgATP. Maximal effects of MgATP were seen at 1 mM. This enhancement by MgATP could not be attributed to protein kinase C. Neomycin was found to inhibit ARFl-regulated PLD activity suggesting the requirement for polyphosphoinositides. We conclude: (i) that many of the observed effects of PMA may be dependent on the presence of the small GTP-binding protein, ARF, and (ii) polyphosphoinositides are required for ARFl-stimulated PLD activity.

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Phospholipase D activation in fibroblast membranes by the α and β isoforms of protein kinase C

Cited by 89 publications

References 33 publications

Phospholipase D Signaling Pathways and Phosphatidic Acid as Therapeutic Targets in Cancer

Phospholipase D Signaling Pathways and Phosphatidic Acid as Therapeutic Targets in Cancer

Isoenzyme-specific Translocation of Protein Kinase C (PKC)βII and not PKCβI to a Juxtanuclear Subset of Recycling Endosomes

ARF1‐regulated phospholipase D in human neutrophils is enhanced by PMA and MgATP

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