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

Ahn, Bong Hyun; Min, Gyesik; Bae, Yoe Sik; Bae, Young‐Seuk; Min, Do Sik

doi:10.1038/emm.2006.7

Cited by 26 publications

(18 citation statements)

References 30 publications

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“…Mutation of S134 to alanine partially decreases EGFstimulated PLD2 activity, but does not inhibit basal PLD2 activity . Casein kinase II is found in complex with both PLD1 (Ganley et al, 2001) and PLD2 (Ahn et al, 2006) and phosphorylates both isozymes. The exact function of the casein kinase II phosphorylation events is unknown, but PLD catalytic activity is unaffected.…”

Section: A Serine and Threonine Phosphorylationmentioning

confidence: 99%

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

2014

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Section: A Serine and Threonine Phosphorylationmentioning

confidence: 99%

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

2014

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“…Cell viability was assessed using a CellTiter 96 Aqueous One Solution cell proliferation assay kit (Promega), as previously described (Ahn et al, 2006). Briefly, 1.0 × 10 3 cells per well were seeded in 96-well plates to which were added a dilution series of doxorubicin and vincristine in triplicate and incubated under standard culture conditions.…”

Section: Cell Proliferation Assaymentioning

confidence: 99%

Depletion of mitochondrial DNA up-regulates the expression of MDR1 gene via an increase in mRNA stability

et al. 2008

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The mutation and reduction of mitochondrial DNA (mtDNA) have been suggested as factors in the carcinogenesis. However, whether the depletion of mtDNA induces multidrug resistance in cancer cells has not been fully investigated. To elucidate the association of cellular mtDNA content and drug resistance, we generated HCT-8 colon cancer cells which revealed a marked decrease in cellular mtDNA and ATP content, concomitant with a lack of mRNAs encoded by mtDNA. The mtDNA-depleted cells showed a decreased sensitivity and accumulation of anti-cancer drugs, suggesting that mtDNA depletion could develop multidrug resistance (MDR) phenotype in HCT-8 cells. We found that the expression level of MDR1 mRNA and its translated product P-glycoprotein was increased in the mtDNA-depleted cells, indicating that the decrease of sensitivity and accumulation of anti-cancer drug in the mtDNA-depleted cells might be due to a substantial increase in the expression of P-glycoprotein. Furthermore, increased expression of MDR1 mRNA and P-glycoprotein was due to an increase of mRNA stability rather than transcriptional activation. Taken together, these results indicate that mtDNA depletion can induce an increased P-glycoprotein expression via an increase of mRNA stability and suggest that the mtDNA depletion in cancer cells plays an important role in the induction of MDR phenotype.

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“…GST-fusion proteins were expressed in Escherichia coli BL21 (DE3) by induction with isopropyl-1-thio--D-galactopyranoside (IPTG) and purified from cleared cellular lysate by affinity chromatography using gluthathione-sepharose beads (Amersham Pharmacia) as described previously (Ahn et al, 2006).…”

Section: Plasmids and Gst Fusion Protein Productionmentioning

confidence: 99%

Identification of novel substrates for human checkpoint kinase Chk1 and Chk2 through genome-wide screening using a consensus Chk phosphorylation motif

Kim

Kim²,

Brown³

et al. 2007

Exp Mol Med

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, mitotic arrest deficient protein 1a; PGC-1 , peroxisome proliferators-activated receptor coactivator-1 ; PP2A, protein phosphatase 2A; PP2A PR130, protein phosphatase 2 regulatory subunit B; Rad51D, RADidation sensitivity abnormal/year RAD-related 51D; ST5, suppression of tumorigenicity 5 AbstractCheckpoint kinase 1 (Chk1) and Chk2 are effector kinases in the cellular DNA damage response and impairment of their function is closely related to tumorigenesis. Previous studies revealed several substrate proteins of Chk1 and Chk2, but identification of additional targets is still important in order to understand their tumor suppressor functions. In this study, we screened novel substrates for Chk1 and Chk2 using substrate target motifs determined previously by an oriented peptide library approach. The potential candidates were selected by genomewide peptide database searches and were examined by in vitro kinase assays. ST5, HDAC5, PGC-1α, PP2A PR130, FANCG, GATA3, cyclin G, Rad51D and MAD1a were newly identified as in vitro substrates for Chk1 and/or Chk2. Among these, HDAC5 and PGC-1α were further analyzed to substantiate the screening results. Immunoprecipitation kinase assay of fulllength proteins and site-directed mutagenesis analysis of the target motifs demonstrated that HDAC5 and PGC-1α were specific targets for Chk1 and/or Chk2 at least in vitro.

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

Cited by 26 publications

References 30 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

Depletion of mitochondrial DNA up-regulates the expression of MDR1 gene via an increase in mRNA stability

Identification of novel substrates for human checkpoint kinase Chk1 and Chk2 through genome-wide screening using a consensus Chk phosphorylation motif

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