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Mol Cell Oncol. 2015 Oct 6;3(2):e1091059. doi: 10.1080/23723556.2015.1091059. eCollection 2016 Mar.

tRNA synthase suppression activates de novo cysteine synthesis to compensate for cystine and glutathione deprivation during ferroptosis.

Author information

1
Department of Biological Sciences, 550 West 120th Street, Columbia University , New York, NY, USA.
2
Department of Biological Sciences, 550 West 120th Street, Columbia University, New York, NY, USA; Department of Chemistry, Howard Hughes Medical Institute, 1208 Northwest Corner Building, MC4846, 550 West 120th Street, Columbia University, New York, NY, USA.

Abstract

Glutathione is a major endogenous reducing agent in cells, and cysteine is a limiting factor in glutathione synthesis. Cysteine is obtained by uptake or biosynthesis, and mammalian cells often rely on either one or the other pathway. Because of the scarcity of glutathione, blockade of cysteine uptake causes oxidative cell death known as ferroptosis. A new study suggests that tRNA synthetase suppression activates the endogenous biosynthesis of cysteine, compensates such cysteine loss, and thus makes cells resistant to ferroptosis.

KEYWORDS:

CARS; Cancer; cysteine; ferroptosis; mechanisms of oncogenesis and tumor progression; methionine

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