NOX4 functions as a mitochondrial energetic sensor coupling cancer metabolic reprogramming to drug resistance View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-10-19

AUTHORS

Karthigayan Shanmugasundaram, Bijaya K. Nayak, William E. Friedrichs, Dharam Kaushik, Ronald Rodriguez, Karen Block

ABSTRACT

The molecular mechanisms that couple glycolysis to cancer drug resistance remain unclear. Here we identify an ATP-binding motif within the NADPH oxidase isoform, NOX4, and show that ATP directly binds and negatively regulates NOX4 activity. We find that NOX4 localizes to the inner mitochondria membrane and that subcellular redistribution of ATP levels from the mitochondria act as an allosteric switch to activate NOX4. We provide evidence that NOX4-derived reactive oxygen species (ROS) inhibits P300/CBP-associated factor (PCAF)-dependent acetylation and lysosomal degradation of the pyruvate kinase-M2 isoform (PKM2). Finally, we show that NOX4 silencing, through PKM2, sensitizes cultured and ex vivo freshly isolated human-renal carcinoma cells to drug-induced cell death in xenograft models and ex vivo cultures. These findings highlight yet unidentified insights into the molecular events driving cancer evasive resistance and suggest modulation of ATP levels together with cytotoxic drugs could overcome drug-resistance in glycolytic cancers. More... »

PAGES

997

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-017-01106-1

DOI

http://dx.doi.org/10.1038/s41467-017-01106-1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1092170309

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29051480


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