Phospholipase D1 Is Phosphorylated and Activated by Protein Kinase C in Caveolin-enriched Microdomains within the Plasma Membrane

Kim, Yong; Han, Jung Min; Han, Byung Ryul; Lee, Kyung Ah; Kim, Jae Ho; Lee, Yong Kyu; Jang, Il Ho; Suh, Pann Ghill; Ryu, Sung Ho

doi:10.1074/jbc.275.18.13621

Cited by 82 publications

(76 citation statements)

References 32 publications

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“…We have reported that PLD can be phosphorylated on tyrosine residues by c-Src and the combination of H2O2 and vanadate Ahn et al, 2003;Kim et al, 2004b). In addition, PLD1 is phosphorylated on serine and threonine residue by PKC Kim et al, 2000). In the present study, we report that CKII is involved in PMA-induced PLD1 and PLD2 activation, phosphorylates PLD2 and interacts with both PLD1 and PLD2.…”

Section: Introductionsupporting

confidence: 47%

Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells

Ahn

Min²,

Bae³

et al. 2006

Exp Mol Med

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Elevated expression of protein casein kinase II (CKII) stimulated basal phospholipase D (PLD) activity as well as PMA-induced PLD activation in human U87 astroglioma cells. Moreover, CKII-selective inhibitor, emodin and apigenin suppressed PMA-induced PLD activation in a dose-dependent manner as well as basal PLD activity, suggesting the involvement of CKII in the activation of both PLD1 and PLD2. CKII was associated with PLD1 and PLD2 in co-transfection experiments. Furthermore, CKII induced serine/threonine phosphorylation of PLD2 in vivo, and the multiple regions of PLD2 were phosphorylated by CKII in vitro kinase assay using glutathione S-transferase-PLD2 fusion protein fragments. Elevated expression of CKII or PLD increased cell proliferation but pretreatment of cells with 1-butanol suppressed CKII-induced cell proliferation. These results suggest that CKII is involved in proliferation of U87 cells at least in part, through stimulation of PLD activity.

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Section: Introductionsupporting

confidence: 47%

Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells

Ahn

Min²,

Bae³

et al. 2006

Exp Mol Med

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“…Cell specific localization has also been noted with PLD isoforms, where Czarny et al (45) have observed PLD2 is preferentially targeted over PLD1 to caveolae/rafts in Chinese hamster ovary cells, HaCaT human keratinocytes, and U937 cells. Kim et al (127,128), on the other hand, have localized PLD1 to DIGs in 3Y1 rat fibroblasts and COS7 cells.…”

Section: Lpp In Signaling Platformsmentioning

confidence: 99%

“…With both cell lines, a proportion of the LPP activity was found associated with the caveolin-enriched domains. Presence of LPP in caveolae/ rafts was anticipated, since studies with other cells have shown that PLD (44,45,127,128) and LPA and S1P receptors (100) can be found associated with DIGs.…”

Section: Lpp In Signaling Platformsmentioning

confidence: 99%

“…A number of other proteins, including the 36-kDa ganglioside G m2 activator protein (required for metabolism of G m2 to G m3 ), have also been implicated in PLD1 regulation (217). PLD1 can be modified by palmitoylation and through phosphorylation by PKC and other kinases, for example, the Rho-dependent Rho kinase, although the effects on activity appear variable (40,128,140,277).…”

Section: Substrates For Lppmentioning

confidence: 99%

“…Interestingly, phorbol ester stimulation of PLD1 in the presence of PIP 2 or PIP 3 does not require ATP but does require the NH 2 -terminal 168 amino acids (hence known as the phorbol ester-binding domain). ATP can further stimulate PLD1 in the presence of phorbol esters through PKC-dependent phosphorylation (128). Certain conserved amino acids at the COOH terminus of PLD1 are essential for full activity (278).…”

Section: Substrates For Lppmentioning

confidence: 99%

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Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

Nanjundan

Possmayer

2003

American Journal of Physiology-Lung Cellular and Molecular Phys

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The lung contains two distinct forms of phosphatidic acid phosphatase (PAP). PAP1 is a cytosolic enzyme that is activated through fatty acid-induced translocation to the endoplasmic reticulum, where it converts phosphatidic acid (PA) to diacylglycerol (DAG) for the biosynthesis of phospholipids and neutral lipids. PAP1 is Mg2+ dependent and sulfhydryl reagent sensitive. PAP2 is a six-transmembrane-domain integral protein localized to the plasma membrane. Because PAP2 degrades sphingosine-1-phosphate (S1P) and ceramide-1-phosphate in addition to PA and lyso-PA, it has been renamed lipid phosphate phosphohydrolase (LPP). LPP is Mg2+independent and sulfhydryl reagent insensitive. This review describes LPP isoforms found in the lung and their location in signaling platforms (rafts/caveolae). Pulmonary LPPs likely function in the phospholipase D pathway, thereby controlling surfactant secretion. Through lowering the levels of lyso-PA and S1P, which serve as agonists for endothelial differentiation gene receptors, LPPs regulate cell division, differentiation, apoptosis, and mobility. LPP activity could also influence transdifferentiation of alveolar type II to type I cells. It is considered likely that these lipid phosphohydrolases have critical roles in lung morphogenesis and in acute lung injury and repair.

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PX Domains

Cheever¹,

Overduin²

2004

Modular Protein Domains

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Phospholipase D1 Is Phosphorylated and Activated by Protein Kinase C in Caveolin-enriched Microdomains within the Plasma Membrane

Cited by 82 publications

References 32 publications

Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells

Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells

Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

PX Domains

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