Non-canonical Glutamate-Cysteine Ligase Activity Protects against Ferroptosis.


Journal

Cell metabolism
ISSN: 1932-7420
Titre abrégé: Cell Metab
Pays: United States
ID NLM: 101233170

Informations de publication

Date de publication:
05 01 2021
Historique:
received: 02 06 2020
revised: 09 10 2020
accepted: 08 12 2020
pubmed: 29 12 2020
medline: 30 11 2021
entrez: 28 12 2020
Statut: ppublish

Résumé

Cysteine is required for maintaining cellular redox homeostasis in both normal and transformed cells. Deprivation of cysteine induces the iron-dependent form of cell death known as ferroptosis; however, the metabolic consequences of cysteine starvation beyond impairment of glutathione synthesis are poorly characterized. Here, we find that cystine starvation of non-small-cell lung cancer cell lines induces an unexpected accumulation of γ-glutamyl-peptides, which are produced due to a non-canonical activity of glutamate-cysteine ligase catalytic subunit (GCLC). This activity is enriched in cell lines with high levels of NRF2, a key transcriptional regulator of GCLC, but is also inducible in healthy murine tissues following cysteine limitation. γ-glutamyl-peptide synthesis limits the accumulation of glutamate, thereby protecting against ferroptosis. These results indicate that GCLC has a glutathione-independent, non-canonical role in the protection against ferroptosis by maintaining glutamate homeostasis under cystine starvation.

Identifiants

pubmed: 33357455
pii: S1550-4131(20)30662-8
doi: 10.1016/j.cmet.2020.12.007
pmc: PMC7839835
mid: NIHMS1655933
pii:
doi:

Substances chimiques

GCLC protein, human EC 6.3.2.2
Glutamate-Cysteine Ligase EC 6.3.2.2

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

174-189.e7

Subventions

Organisme : NCI NIH HHS
ID : R01 CA189623
Pays : United States
Organisme : NCI NIH HHS
ID : R37 CA230042
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA076292
Pays : United States
Organisme : NIAID NIH HHS
ID : U01 AI148118
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK123738
Pays : United States

Commentaires et corrections

Type : CommentIn

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Interests I.S.H. is a consultant for Ono Pharma USA. E.S. is an inventor of intellectual property related cyst(e)inase, and has an equity interest in Aeglea Biotherapeutics, a company pursuing the commercial development of cyst(e)inase. These companies had no role in funding or the design of this study.

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Auteurs

Yun Pyo Kang (YP)

Department of Cancer Physiology, H. Lee. Moffitt Cancer Center, Tampa, FL 33612, USA.

Andrea Mockabee-Macias (A)

Department of Cancer Physiology, H. Lee. Moffitt Cancer Center, Tampa, FL 33612, USA.

Chang Jiang (C)

Department of Cancer Physiology, H. Lee. Moffitt Cancer Center, Tampa, FL 33612, USA.

Aimee Falzone (A)

Department of Cancer Physiology, H. Lee. Moffitt Cancer Center, Tampa, FL 33612, USA.

Nicolas Prieto-Farigua (N)

Department of Cancer Physiology, H. Lee. Moffitt Cancer Center, Tampa, FL 33612, USA.

Everett Stone (E)

Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.

Isaac S Harris (IS)

University of Rochester Medical Center, Rochester, NY 14642, USA.

Gina M DeNicola (GM)

Department of Cancer Physiology, H. Lee. Moffitt Cancer Center, Tampa, FL 33612, USA. Electronic address: gina.denicola@moffitt.org.

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Classifications MeSH