Role of the N-terminal hydrophobic residues of DGKε in targeting the endoplasmic reticulum

Matsui, Hiroki; Hozumi, Yasukazu; Tanaka, Toshiaki; Okada, Masashi; Nakano, Tomoyuki; Suzuki, Yusuke; Iseki, Ken; Kakehata, Seiji; Topham, Matthew K.; Goto, Kaoru

doi:10.1016/j.bbalip.2014.07.007

Cited by 27 publications

(25 citation statements)

References 61 publications

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“…Fluorescence microscopy and sub-cellular fractionation experiments have demonstrated that DGKe in cells is bound to membranes and is localized at the endoplasmic reticulum (ER) and plasma membrane (PM) (Decaffmeyer et al, 2008;Matsui Abbreviations: DAG, diacylglycerol; DGK, diacylglycerol kinase; DGKe, the epsilon isoform of diacylglycerol kinase; DOG, 1,2-dioleoyl-glycerol; DOPC, 1,2-dioleoyl-phosphatidylcholine; ECS, electroconvulsive shock; ER, endoplasmic reticulum; HD, Huntington disease; Htt, Huntingtin protein; KO, knockout; LTP, long term potentiation; MEF, mouse embryo fibroblast; PA, phosphatidic acid; PI, phosphatidylinositol; PI-cycle, metabolic cycle to synthesize PI; PIP 2 , phosphatidylinositol-4,5-bisphosphate; PIP n , all forms of phosphorylated PI; PKC, protein kinase C; PM, plasma membrane; P-motif, phosphate binding motif; SAG, 1-stearoyl-2-arachidonoyl-glycerol; SAPA, 1-stearoyl-2-arachidonoyl-PA; SLG, 1-stearoyl-2-linoleoyl-glycerol; SLPA, 1-stearoyl-2-linoleoyl-PA; NMR, nuclear magnetic resonance; WT, wild-type. Kobayashi et al, 2007).…”

Section: Membrane Penetrationmentioning

confidence: 99%

Molecular properties of diacylglycerol kinase-epsilon in relation to function

Jennings

Doshi

D’Souza

et al. 2015

Chemistry and Physics of Lipids

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Section: Membrane Penetrationmentioning

confidence: 99%

Molecular properties of diacylglycerol kinase-epsilon in relation to function

Jennings

Doshi

D’Souza

et al. 2015

Chemistry and Physics of Lipids

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“…3b). Because our previous study showed that DGKε localized to the endoplasmic reticulum (ER; Matsui et al 2014), we conducted double-immunolabeling experiments with an antibody against calregulin, a marker for the ER. Puncta labeled for DGKε were only partly colocalized with calregulin staining (Fig.…”

Section: Zona Glomerulosamentioning

confidence: 99%

Expression and localization of the diacylglycerol kinase family and of phosphoinositide signaling molecules in adrenal gland

et al. 2015

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Adrenal glands play a central role in the secretion of steroid hormones and catecholamines. Previous studies have revealed that molecules engaged in phosphoinositide (PI) turnover are expressed in the adrenal gland, suggesting the importance of PI signaling in adrenal signal transduction. Diacylglycerol kinase (DGK) catalyzes the phosphorylation of diacylglycerol (DG), a major second messenger in the PI signaling cascade. The DGK family is expressed in distinct patterns in endocrine organs at the mRNA and protein levels. Nevertheless, little is known about the characteristics and morphological aspects of DGKs in the adrenal gland. We have performed immunohistochemical analyses to investigate the expression and localization of DGK isozymes, together with PI signaling molecules, in the adrenal gland at the protein level. Our results show that the DGK family and a set of PI signaling molecules are expressed intensely in zona glomerulosa cells and medullary chromaffin cells in the adrenal gland. In adrenal cells, DGKγ localizes to the Golgi complex, DGKε to the plasma membrane, and DGKζ to the nucleus. These findings show the distinct expression and subcellular localization of DGK isozymes and PI signaling molecules in the adrenal gland, suggesting that each DGK isozyme has a role in signal transduction in adrenal cells, especially in the zona glomerulosa and medulla.

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“…Control siRNA (All stars negative control) was purchased from Qiagen (Valencia, CA). The siRNAs were transfected using RNAiMAX (Life Technologies) according to the manufacturer's instructions (10,16).…”

Section: Resultsmentioning

confidence: 99%

<b>Orotate phosphoribosyltransferase localizes to the Golgi complex and its expression levels affect the sensitivity to anti-cancer drug 5-fluor</b><b>ouracil </b>

et al. 2015

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Orotate phosphoribosyltransferase (OPRT) is engaged in de novo pyrimidine synthesis. It catalyzes oronitine to uridine monophosphate (UMP), which is used for RNA synthesis. De novo pyrimidine synthesis has long been known to play an important role in providing DNA/RNA precursors for rapid proliferative activity of cancer cells. Furthermore, chemotherapeutic drug 5-fluorouracil (5-FU) is taken up into cancer cells and is converted to 5-fluoro-UMP (FUMP) by OPRT or to 5-fluoro-dUMP (FdUMP) through intermediary molecules by thymidine phosphorylase. These 5-FU metabolites are misincorporated into DNA/RNA, thereby producing dysfunction of these information processing. However, it remains unclear how the subcellular localization of OPRT and how its variable expression levels affect the response to 5-FU at the cellular level. In this study, immunocytochemical analysis reveals that OPRT localizes to the Golgi complex. Results also show that not only overexpression but also downregulation of OPRT render cells susceptible to 5-FU exposure, but it has no effect on DNA damaging agent doxorubicin. This study provides clues to elucidate the cellular response to 5-FU chemotherapy in relation to the OPRT expression level.

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Role of the N-terminal hydrophobic residues of DGKε in targeting the endoplasmic reticulum

Cited by 27 publications

References 61 publications

Molecular properties of diacylglycerol kinase-epsilon in relation to function

Molecular properties of diacylglycerol kinase-epsilon in relation to function

Expression and localization of the diacylglycerol kinase family and of phosphoinositide signaling molecules in adrenal gland

<b>Orotate phosphoribosyltransferase localizes to the Golgi complex and its expression levels affect the sensitivity to anti-cancer drug 5-fluor</b><b>ouracil </b>

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