Pyruvate carboxylation enables growth of SDH-deficient cells by supporting aspartate biosynthesis View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-10

AUTHORS

Simone Cardaci, Liang Zheng, Gillian MacKay, Niels J. F. van den Broek, Elaine D. MacKenzie, Colin Nixon, David Stevenson, Sergey Tumanov, Vinay Bulusu, Jurre J. Kamphorst, Alexei Vazquez, Stewart Fleming, Francesca Schiavi, Gabriela Kalna, Karen Blyth, Douglas Strathdee, Eyal Gottlieb

ABSTRACT

Succinate dehydrogenase (SDH) is a heterotetrameric nuclear-encoded complex responsible for the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Loss-of-function mutations in any of the SDH genes are associated with cancer formation. However, the impact of SDH loss on cell metabolism and the mechanisms enabling growth of SDH-defective cells are largely unknown. Here, we generated Sdhb-ablated kidney mouse cells and used comparative metabolomics and stable-isotope-labelling approaches to identify nutritional requirements and metabolic adaptations to SDH loss. We found that lack of SDH activity commits cells to consume extracellular pyruvate, which sustains Warburg-like bioenergetic features. We further demonstrated that pyruvate carboxylation diverts glucose-derived carbons into aspartate biosynthesis, thus sustaining cell growth. By identifying pyruvate carboxylase as essential for the proliferation and tumorigenic capacity of SDH-deficient cells, this study revealed a metabolic vulnerability for potential future treatment of SDH-associated malignancies. More... »

PAGES

1317-1326

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ncb3233

    DOI

    http://dx.doi.org/10.1038/ncb3233

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1045558442

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/26302408


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