Positive Regulation of Apoptosis Signal-regulating Kinase 1 by hD53L1

Cho, Sayeon; Ko, Hyung Mun; Kim, Jeong‐Min; Lee, Jung A.; Park, Jae Eun; Jang, Mi; Park, Sung Goo; Lee, Do Hee; Ryu, Seong Eon; Park, Byoung Chul

doi:10.1074/jbc.m305758200

Cited by 33 publications

(27 citation statements)

References 44 publications

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“…We have obtained and identified positive clones, some of which (for example MAPKKK6 and 14-3-3 proteins) have already been reported to interact with ASK1 (Wang et al, 1998;Zhang et al, 1999). One of two de novo interacting groups was identified as human D53-like 1 (hD53L1) and its role in the regulation of ASK1 activity was published elsewhere (Cho et al, 2004). The other group contained two independent clones of GSPT1, both of which included a common C-terminal segment (residues 444-637).…”

Section: Resultsmentioning

confidence: 99%

“…For most transient transfections of expression plasmids, 1.4 Â 10 6 cells were plated in a 60 mm cell culture plate, grown overnight, and transfected with appropriate methods as described previously (Cho et al, 2004).…”

Section: Transfectionmentioning

confidence: 99%

“…The C-terminally HA-tagged GSPT1 and FLAG-tagged GSPT1 expression plasmids were generated by PCR and subcloned into pcDNA3.1/Zeo (Invitrogen). Constructions of FLAG-ASK1, FLAG-ASK-K and FLAG-ASK-C expression plasmids were described previously (Cho et al, 2004). FLAG-ASK1-S967A expression plasmid was constructed by PCR using FLAG-ASK1 as a template.…”

Section: Plasmid Constructions Ha-ask1 and Ask1mentioning

confidence: 99%

“…After 48 h of transfection, cell lysates were prepared and immunoprecipitated as previously described (Cho et al, 2004). The bound proteins were eluted with the SDS-PAGE sample buffer and were separated by SDS-PAGE, followed by immunoblotting with anti-FLAG M2 antibody or an anti-HA antibody.…”

Section: Plasmid Constructions Ha-ask1 and Ask1mentioning

confidence: 99%

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G1 to S phase transition protein 1 induces apoptosis signal-regulating kinase 1 activation by dissociating 14-3-3 from ASK1

et al. 2007

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Apoptosis signal-regulating kinase 1 (ASK1), a member of the mitogen-activated protein kinase kinase kinase family, plays a critical role in mediating apoptosis signals initiated by a variety of death stimuli such as hydrogen peroxide and tumor necrosis factor-a. Owing to its critical role in inducing apoptosis, the activity of ASK1 is tightly regulated by various mechanisms such as post-translational modifications and protein-protein interactions. Here we describe the identification of G 1 to S phase transition protein 1 (GSPT1), which is associated with protein translation, as a regulator of ASK1. GSPT1 interacts with ASK1 and enhances ASK1-induced apoptotic activity through the activation of caspase-3. In vitro kinase assay data show that GSPT1 enhances ASK1 autophosphorylation and its kinase activity. Cell cycledependent GSPT1 induction and small interfering RNA analyses show that ASK1 autophosphorylation is dependent on the expression level of endogenous GSPT1 in cells. GSPT1 inhibits the binding of ASK1 to the 14-3-3 protein, an ASK1 inhibitor, while GSPT1 has no effect on the interaction between ASK1 and TRAF2, a C-terminalbinding activator of ASK1. Thus, our results reveal a novel role of GSPT1 in the regulation of ASK1-mediated apoptosis.

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Section: Resultsmentioning

confidence: 99%

Section: Transfectionmentioning

confidence: 99%

Section: Plasmid Constructions Ha-ask1 and Ask1mentioning

confidence: 99%

Section: Plasmid Constructions Ha-ask1 and Ask1mentioning

confidence: 99%

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G1 to S phase transition protein 1 induces apoptosis signal-regulating kinase 1 activation by dissociating 14-3-3 from ASK1

et al. 2007

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“…ASK1 is regulated either positively or negatively depending on its binding proteins. 12,13,15,[18][19][20][21][22][23][24][25] ASK1 is regulated by phosphorylation at several Ser/Thr/Tyr residues. Phosphorylation at Thr-838 leads to activation of ASK1, whereas phosphorylation at Ser-83, Ser-967, or Ser-1034 inactivates ASK1.…”

mentioning

confidence: 99%

Cell cycle-dependent Cdc25C phosphatase determines cell survival by regulating apoptosis signal-regulating kinase 1

Cho

Park

et al. 2015

Cell Death Differ

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Cdc25C (cell division cycle 25C) phosphatase triggers entry into mitosis in the cell cycle by dephosphorylating cyclin B-Cdk1. Cdc25C exhibits basal phosphatase activity during interphase and then becomes activated at the G 2 /M transition after hyperphosphorylation on multiple sites and dissociation from 14-3-3. Although the role of Cdc25C in mitosis has been extensively studied, its function in interphase remains elusive. Here, we show that during interphase Cdc25C suppresses apoptosis signal-regulating kinase 1 (ASK1), a member of mitogen-activated protein (MAP) kinase kinase kinase family that mediates apoptosis. Cdc25C phosphatase dephosphorylates phospho-Thr-838 in the activation loop of ASK1 in vitro and in interphase cells. In addition, knockdown of Cdc25C increases the activity of ASK1 and ASK1 downstream targets in interphase cells, and overexpression of Cdc25C inhibits ASK1-mediated apoptosis, suggesting that Cdc25C binds to and negatively regulates ASK1. Furthermore, we showed that ASK1 kinase activity correlated with Cdc25C activation during mitotic arrest and enhanced ASK1 activity in the presence of activated Cdc25C resulted from the weak association between ASK1 and Cdc25C. In cells synchronized in mitosis following nocodazole treatment, phosphorylation of Thr-838 in the activation loop of ASK1 increased. Compared with hypophosphorylated Cdc25C, which exhibited basal phosphatase activity in interphase, hyperphosphorylated Cdc25C exhibited enhanced phosphatase activity during mitotic arrest, but had significantly reduced affinity to ASK1, suggesting that enhanced ASK1 activity in mitosis was due to reduced binding of hyperphosphorylated Cdc25C to ASK1. These findings suggest that Cdc25C negatively regulates proapoptotic ASK1 in a cell cycle-dependent manner and may play a role in G 2 /M checkpointmediated apoptosis.

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Prognostic role of TPD52 in acute myeloid leukemia: A retrospective multicohort analysis

Han

Kim

et al. 2018

J of Cellular Biochemistry

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Generating accurate prognoses is extremely important for treating patients with cancer. Prognostic prediction based on messenger RNA (mRNA) expression has shown superior clinical value to other markers for some cancers but is not currently used for acute myeloid leukemia (AML). Lipid metabolism is associated with biological aspects of cancer progression, including massive proliferation, and abnormal signaling. Moreover, abnormalities in lipid metabolism have prognostic significance. Patients with AML display abnormalities in sphingolipid metabolism and fatty acid oxidation. TPD52 is a regulator of lipid metabolism and plays a role in the formation of lipid droplets and fatty acid storage. Although the prognostic significance of TPD52 expression has been reported for many types of cancer, it has not yet been assessed in patients with AML. Therefore, the aim of the current study was to assess the prognostic significance of TPD52 in AML using three independent AML cohorts: one from The Cancer Genome Atlas (TGCA; n = 142) and two from the National Center for Biotechnology Information: GSE12417 (GPL96-97; n = 162) and GSE12417 (GPL570; n = 78). TPD52 was found to be overexpressed in patients with AML (GSE84881; n = 23). The Kaplan-Meier curve revealed that TPD52 overexpression was associated with a poor prognosis for patients with AML with good discrimination ( P = 0.013, P = 0.005, and P = 0.032 for the TGCA, GSE12417, and GSE12417, respectively). Analysis of C-indices and area under the receiver operating characteristic curve values further supported this discriminative ability. Moreover, multivariate analysis confirmed the prognostic significance of TPD52 expression levels ( P = 0.0196). These results suggest that the TPD52 mRNA level is a potential biomarker for AML.

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Positive Regulation of Apoptosis Signal-regulating Kinase 1 by hD53L1

Cited by 33 publications

References 44 publications

G1 to S phase transition protein 1 induces apoptosis signal-regulating kinase 1 activation by dissociating 14-3-3 from ASK1

G1 to S phase transition protein 1 induces apoptosis signal-regulating kinase 1 activation by dissociating 14-3-3 from ASK1

Cell cycle-dependent Cdc25C phosphatase determines cell survival by regulating apoptosis signal-regulating kinase 1

Prognostic role of TPD52 in acute myeloid leukemia: A retrospective multicohort analysis

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