Mouse NIPK interacts with ATF4 and affects its transcriptional activity

Örd, Daima; Örd, Tönis

doi:10.1016/s0014-4827(03)00070-3

Cited by 79 publications

(36 citation statements)

References 73 publications

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“…Interestingly, the ATF4-CHOP pathway has been previously shown to induce TRB3 expression under conditions of ER stress, and that TRB3 can reciprocally repress the function of ATF4 and CHOP [22,36]. Specifically, Ohoka et al [22] showed that CHOP and ATF4 cooperate to activate the TRB3 promoter.…”

Section: Discussionmentioning

confidence: 99%

Palmitate Induces TRB3 Expression and Promotes Apoptosis in Human Liver Cells

Yan

Wang

Xiao

et al. 2014

Cell Physiol Biochem

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Background/Aims: Parenteral nutrition-associated liver disease (PNALD) is a major complication for patients who require long-term parenteral nutrition. Treatment options for PNALD are limited and its pathogenesis is poorly understood. Tribbles homolog 3 (TRB3) is a pseudokinase that modulates many signal transduction cascades and may be involved in the pathogenesis of PNALD. The aim of this study was to examine the role of TRB3 in palmitate-induced endoplasmic reticulum (ER) stress, in the human liver cell line L02. Methods: L02 cells were treated with palmitate, and its effect on cell viability, mitochondrial membrane potential, apoptosis and TRB3 expression were assessed. The role of TRB3 was also studied using transient overexpression of TRB3 in L02 cells, as well as its interaction with Akt signaling. Results: We found that palmitate induced ER stress and apoptosis in L02 cells. Palmitate-associated ER stress was accompanied by a significant induction of TRB3 expression at the mRNA and protein level. Overexpression of TRB3 potentiated the deleterious effects of palmitate, which was associated with decreased levels of phospho-Akt. Conclusions: TRB3 is an important mediator of palmitate-induced apoptosis in human liver cells, suggesting that it may also be involved in the molecular mechanism underlying PNALD.

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Section: Discussionmentioning

confidence: 99%

Palmitate Induces TRB3 Expression and Promotes Apoptosis in Human Liver Cells

Yan

Wang

Xiao

et al. 2014

Cell Physiol Biochem

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“…TRB3 (alias TRIB3, NIPK, SKIP3), a member of the Tribbles family of pseudokinases, interacts with several transcription factors (ATF4 (Bowers et al, 2003;Örd and Örd, 2003), CHOP (Ohoka et al, 2005), NF-κB (Wu et al, 2003), C/EBPβ (Bezy et al, 2007)), protein kinases (Akt/PKB (Du et al, 2003), MAPK kinases MEK1 and MKK7 (Kiss-Toth et al, 2004)) and other proteins (E3 ubiquitin ligase COP1 (Qi et al, 2006), Smad ubiquitin regulatory factor 1 (Chan et al, 2007), nuclear protein CtIP (Xu et al, 2007)), and has been implicated in the regulation of cellular stress response, viability and metabolism. TRB3 has attracted attention for its potential role in medical conditions: molecular and epidemiologic studies, as well as the examination of disease models, have linked TRB3 to insulin resistance (Du et al, 2003;Koo et al, 2004;Prudente et al, 2005;He et al, 2006;Yao and Nyomba, 2008), cardiovascular disease (Prudente et al, 2005) and diabetes (Prudente et al, 2009), and the elevated expression of TRB3 has been reported in many cancer cell lines and primary tumors (Bowers et al, 2003;Xu et al, 2007), and in cancer cells treated with antitumoral agents (Carracedo et al, 2006a,b).…”

Section: Introductionmentioning

confidence: 99%

Human TRB3 is upregulated in stressed cells by the induction of translationally efficient mRNA containing a truncated 5′-UTR

Örd

Kõivomägi

et al. 2009

Gene

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“…Another example of TRIB-dependent degradation of target proteins in cancer is represented by Activating transcription factor 4 (ATF4) which occurs during hypoxia in human tumour cells overexpressing TRIB3 [28] . Interestingly, the murine ortholog of TRIB3 Neuronal cell death-inducible putative kinase (NIPK) has also been associated with downregulation of ATF4 transcriptional activity, but in absence of proteolytic degradation [29] . The protein interaction of ATF4 with TRIB2 or TRIB1 as not been reported.…”

Section: Trib2: the Ruler Of E3 Ubiquitin Ligase Activitiesmentioning

confidence: 99%

TRIB2 and the ubiquitin proteasome system in cancer

Salomé

Campos

Keeshan

2015

Biochemical Society Transactions

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Tribbles family of pseudokinase proteins are known to mediate the degradation of target proteins in Drosophila and mammalian systems. The main protein proteolysis pathway in eukaryotic cells is the ubiquitin proteasome system (UPS). The tribbles homolog 2 (TRIB2) mammalian family member has been well characterized for its role in murine and human leukaemia, lung and liver cancer. One of the most characterized substrates for TRIB2-mediated degradation is the myeloid transcription factor CCAAT enhancer binding protein α (C/EBPα). However, across a number of cancers, the molecular interactions that take place between TRIB2 and factors involved in the UPS are varied and have differential downstream effects. This review summarizes our current knowledge of these interactions and how this information is important for our understanding of TRIB2 in cancer.

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Mouse NIPK interacts with ATF4 and affects its transcriptional activity

Cited by 79 publications

References 73 publications

Palmitate Induces TRB3 Expression and Promotes Apoptosis in Human Liver Cells

Palmitate Induces TRB3 Expression and Promotes Apoptosis in Human Liver Cells

Human TRB3 is upregulated in stressed cells by the induction of translationally efficient mRNA containing a truncated 5′-UTR

TRIB2 and the ubiquitin proteasome system in cancer

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