Evidence map›Paper›PMID 42191797›Full record

ArticleCommunications biology2026

Dual targeting of glutamine metabolism and lysosomal function in eliminating drug-tolerant KRAS-mutant cancer cells.

Hiroki Furukawa, Keitaro Umezawa, Yuchen Sun, Hinata Chiba, Marin Kubonishi, Hayato Naito, Yuri Miura, Kousei Ito, Shigeki Aoki

Abstract read
In one paragraph

Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Hiroki FurukawaLaboratory of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, Japan.
Keitaro UmezawaResearch Team for Mechanism of Aging, Tokyo Metropolitan Institute for Geriatrics and Gerontology, Tokyo, Japan.ORCID 0000-0002-2380-4453
Yuchen SunDivision of Medicinal Safety Science, National Institute of Health Sciences, Kawasaki, Japan.
Hinata ChibaLaboratory of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, Japan.
Marin KubonishiLaboratory of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, Japan.
Hayato NaitoLaboratory of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, Japan.
Yuri MiuraResearch Team for Mechanism of Aging, Tokyo Metropolitan Institute for Geriatrics and Gerontology, Tokyo, Japan.
Kousei ItoLaboratory of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, Japan.
Shigeki AokiLaboratory of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, Japan. aokishigeki@chiba-u.jp.ORCID 0000-0003-2821-0651

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) 22K19368MEXT | Japan Society for the Promotion of Science (JSPS) 25K22515
6 · The paper itself

Abstract

KRAS inhibitors are reshaping the cancer-treatment landscape; however, durable responses remain limited by drug-tolerant persister cells that survive initial therapy and drive relapse. We show that KRAS-mutant pancreatic and lung cancer cells enter a reversible drug-tolerant (TR) state upon KRAS inhibition, marked by proliferative arrest and extensive metabolic adaptation. Integrated proteomic and metabolomic analyses reveal lysosome-linked remodeling and relatively broad metabolic reprogramming in TR cells. Dual blockade of glutamine metabolism and lysosome-associated processes selectively compromises TR-cell viability under KRAS inhibition, which is rescued by α-ketoglutarate (α-KG). N-acetyl-L-cysteine phenocopies the rescue, and α-KG supplementation lowers intracellular reactive oxygen species levels, supporting a model in which α-KG acts predominantly as a redox-supportive metabolite rather than a Tricarboxylic Acid Cycle intermediate, in the TR state, with lysosome-associated processes contributing to redox balance. These findings define drug-tolerant redox vulnerability and provide a rationale for co-targeting glutamine metabolism and lysosome-associated processes during KRAS inhibitor therapy.

Indexed as

Drug Resistance, NeoplasmGlutamineLung NeoplasmsLysosomesMutationPancreatic NeoplasmsProto-Oncogene Proteins p21(ras)Antineoplastic AgentsCell Line, TumorHumansKetoglutaric AcidsMetabolic ReprogrammingReactive Oxygen SpeciesAntineoplastic AgentsGlutamineKetoglutaric AcidsKRAS protein, humanProto-Oncogene Proteins p21(ras)Reactive Oxygen Species

Identifiers

PMID42191797
PMCPMC13486645

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.