ARD1 binding to RIP1 mediates doxorubicin-induced NF-κB activation

Park, Jonggyu; Kanayama, Atsuhiro; Yamamoto, Kazuo; Miyamoto, Yusei

doi:10.1016/j.bbrc.2012.04.150

Cited by 23 publications

(27 citation statements)

References 20 publications

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“…Yet, another mechanism presented by Shin and colleagues reports that Naa10 inhibits cell motility by direct binding of MLCK and following acetylation of K608, thereby inactivating the ability of MLCK to phosphorylate MLC [158]. Studies by Park et al showed Naa10 as required for doxorubicin NF-κB activation by its interaction with the receptor-interacting protein 1 (RIP1) [159]. Recently, NAA10 expression in colon cancer was found regulated by microRNAs, targeting NAA10 for degradation [160].…”

Section: Naa10 -A Tumor Suppressor?mentioning

confidence: 96%

The world of protein acetylation

Drazic

Myklebust

Ree

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

648

562

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Acetylation is one of the major post-translational protein modifications in the cell, with manifold effects on the protein level as well as on the metabolome level. The acetyl group, donated by the metabolite acetyl-coenzyme A, can be co- or post-translationally attached to either the α-amino group of the N-terminus of proteins or to the ε-amino group of lysine residues. These reactions are catalyzed by various N-terminal and lysine acetyltransferases. In case of lysine acetylation, the reaction is enzymatically reversible via tightly regulated and metabolism-dependent mechanisms. The interplay between acetylation and deacetylation is crucial for many important cellular processes. In recent years, our understanding of protein acetylation has increased significantly by global proteomics analyses and in depth functional studies. This review gives a general overview of protein acetylation and the respective acetyltransferases, and focuses on the regulation of metabolic processes and physiological consequences that come along with protein acetylation.

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Section: Naa10 -A Tumor Suppressor?mentioning

confidence: 96%

The world of protein acetylation

Drazic

Myklebust

Ree

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

648

562

View full text Add to dashboard Cite

show abstract

“…Park and colleagues showed that siRNA-mediated knockdown attenuated, or overexpression of Naa10 increased, respectively, doxorubicin-induced RIP1/PIDD/NEMO complex formation, NEMO ubiquitination and NF-κB activation in HEK293 cells (Park et al, 2012). Specifically, Naa10 binds RIP1 via its acetyltransferase domain (aa45–130); however, the N-terminus as well a functional active acetyltransferase domain of Naa10 are necessary to induce NF-κB activation (Park et al, 2012).…”

Section: Mammalsmentioning

confidence: 99%

Section: Mammalsmentioning

confidence: 99%

“…Specifically, Naa10 binds RIP1 via its acetyltransferase domain (aa45–130); however, the N-terminus as well a functional active acetyltransferase domain of Naa10 are necessary to induce NF-κB activation (Park et al, 2012). TNFα-induced NFκB activation was not affected by Naa10 knockdown (Yi et al, 2011; Park et al, 2012). In line with that, in vitro pull-down and co-immunoprecipitation assays in three cancer cell lines (RKO, H1299 and A549) showed that Naa10 directly interacts with NF-κB (RelA/p56) and contributes in NF-κB transcriptional activation of MCL1 (induced myeloid leukemia cell differentiation protein 1), thereby protecting cells from apoptosis (Xu et al, 2012).…”

Section: Mammalsmentioning

confidence: 99%

“…In humans, Naa10 225 is absent and Naa10 235 was found to be evenly distributed in both cytoplasm and nucleus of HeLa and HT1080 cells as seen by immunofluorescence, confocal microscopy, and cell fractionation (Chun et al, 2007). Naa10 could be detected in nuclear fractions of doxorubicin treated HEK293 cells whereas a deletion construct lacking amino acids 1–35 could not be detected suggesting that a nuclear localization signal (NLS) resides in the N-terminal part of Naa10 (Park et al, 2012). Sequence analysis had previously identified a putative NLS more C-terminally in Naa10 between residues 78 and 83 (KRSHRR) (Arnesen et al, 2005a).…”

Section: Introductionmentioning

confidence: 99%

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The biological functions of Naa10 — From amino-terminal acetylation to human disease

Dörfel

Lyon

2015

Gene

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N-terminal acetylation (NTA) is one of the most abundant protein modifications known, and the N-terminal acetyltransferase (NAT) machinery is conserved throughout all Eukarya. Over the past 50 years, the function of NTA has begun to be slowly elucidated, and this includes the modulation of protein–protein interaction, protein-stability, protein function, and protein targeting to specific cellular compartments. Many of these functions have been studied in the context of Naa10/NatA; however, we are only starting to really understand the full complexity of this picture. Roughly, about 40% of all human proteins are substrates of Naa10 and the impact of this modification has only been studied for a few of them. Besides acting as a NAT in the NatA complex, recently other functions have been linked to Naa10, including post-translational NTA, lysine acetylation, and NAT/KAT-independent functions. Also, recent publications have linked mutations in Naa10 to various diseases, emphasizing the importance of Naa10 research in humans. The recent design and synthesis of the first bisubstrate inhibitors that potently and selectively inhibit the NatA/Naa10 complex, monomeric Naa10, and hNaa50 further increases the toolset to analyze Naa10 function.

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Impact of peroxisome proliferator activated receptor agonist drugs in a model of nephrotoxicity in rats

Ali

Saad

El-Rhman

et al. 2023

J Biochem & Molecular Tox

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Doxorubicin (DOX) is one of the basic anticancer drugs, nonetheless its use is restricted due to noxious side effects. Kidney failure is one of the main side effects that restrict its medical use. The current study assessed the nephroprotective effects of fenofibrate and pioglitazone against the renal injury induced by doxorubicin in rats and illustrated the probable mechanisms underlying these protective effects. For this purpose, Male Sprague-Dawley rats weighing (200-230 g) were allocated into seven groups treated for 15 days as following: control (50% corn oil + 50% DMSO p.o), fenofibrate (100 mg/kg p.o) and pioglitazone (10 mg/kg p.o) as well as four groups of DOX (15 mg/kg i.p on 11th day). DOX groups included DOX alone and DOX with protective drugs fenofibrate, pioglitazone or both of them. As a result of doxorubicin nephrotoxicity; serum creatinine and blood urea nitrogen were remarkably elevated. Moreover, renal glutathione was significantly reduced while tissue lipid peroxidation malondialdehyde, tumor necrosis factor-α, nuclear factor-kappa B p65 (NF-κB p65), interleukin-1β, p38 mitogen activated protein kinase (p38-MAPK) and caspase-3 (Casp-3) were significantly augmented. Treatment with fenofibrate and pioglitazone either alone or in combination markedly attenuated DOX-induced injury by suppression of oxidative stress, inflammation and apoptosis. The above-mentioned biochemical markers were affirmed by histological assessment. In conclusion, fenofibrate, pioglitazone, and their combination possess potential prophylactic effects against doxorubicin-induced renal injury through modulation of p38-MAPK/ NF-κB p65 pathway with superiority to the combination.

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ARD1 binding to RIP1 mediates doxorubicin-induced NF-κB activation

Cited by 23 publications

References 20 publications

The world of protein acetylation

The world of protein acetylation

The biological functions of Naa10 — From amino-terminal acetylation to human disease

Impact of peroxisome proliferator activated receptor agonist drugs in a model of nephrotoxicity in rats

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