_version_ 1868266234591576064
author Fan, Yizeng
Wang, Yuzhao
Dan, Weichao
Zhang, Yilei
Nie, Li
Ma, Zhiqiang
Zhuang, Yanxin
Liu, Bo
Li, Mengxing
Liu, Tianjie
Wang, Zixi
Ye, Leihong
Wei, Yi
Lei, Yuzeshi
Guo, Chendong
An, Jiale
Wang, Chi
Zhang, Yulin
Zeng, Jin
Wei, Wenyi
Gan, Boyi
Li, Lei
author_facet Fan, Yizeng
Wang, Yuzhao
Dan, Weichao
Zhang, Yilei
Nie, Li
Ma, Zhiqiang
Zhuang, Yanxin
Liu, Bo
Li, Mengxing
Liu, Tianjie
Wang, Zixi
Ye, Leihong
Wei, Yi
Lei, Yuzeshi
Guo, Chendong
An, Jiale
Wang, Chi
Zhang, Yulin
Zeng, Jin
Wei, Wenyi
Gan, Boyi
Li, Lei
Fan, Yizeng
Wang, Yuzhao
Dan, Weichao
Zhang, Yilei
Nie, Li
Ma, Zhiqiang
Zhuang, Yanxin
Liu, Bo
Li, Mengxing
Liu, Tianjie
Wang, Zixi
Ye, Leihong
Wei, Yi
Lei, Yuzeshi
Guo, Chendong
An, Jiale
Wang, Chi
Zhang, Yulin
Zeng, Jin
Wei, Wenyi
Gan, Boyi
Li, Lei
collection PubMed - marine biology
contents PRMT5-mediated arginine methylation stabilizes GPX4 to suppress ferroptosis in cancer. Fan, Yizeng Wang, Yuzhao Dan, Weichao Zhang, Yilei Nie, Li Ma, Zhiqiang Zhuang, Yanxin Liu, Bo Li, Mengxing Liu, Tianjie Wang, Zixi Ye, Leihong Wei, Yi Lei, Yuzeshi Guo, Chendong An, Jiale Wang, Chi Zhang, Yulin Zeng, Jin Wei, Wenyi Gan, Boyi Li, Lei Ferroptosis Protein-Arginine N-Methyltransferases Humans Animals Phospholipid Hydroperoxide Glutathione Peroxidase Methylation Arginine Mice Neoplasms F-Box-WD Repeat-Containing Protein 7 Cell Line, Tumor Female Ubiquitination Mice, Nude Mice, Inbred BALB C HEK293 Cells The activation of ferroptosis has shown great potential for cancer therapy from an unconventional perspective, but revealing the mechanisms underlying the suppression of tumour-intrinsic ferroptosis to promote tumorigenesis remains a challenging task. Here we report that methionine is metabolized into S-adenosylmethionine, which functions as a methyl-group donor to trigger symmetric dimethylation of glutathione peroxidase 4 (GPX4) at the conserved arginine 152 (R152) residue, along with a prolonged GPX4 half-life. Inhibition of protein arginine methyltransferase 5 (PRMT5), which catalyses GPX4 methylation, decreases GPX4 protein levels by impeding GPX4 methylation and increasing ferroptosis inducer sensitivity in vitro and in vivo. This methylation prevents Cullin1-FBW7 E3 ligase binding to GPX4, thereby abrogating the ubiquitination-mediated GPX4 degradation. Notably, combining PRMT5 inhibitor treatment with ferroptotic therapies markedly suppresses tumour progression in mouse tumour models. In addition, the levels of GPX4 are negatively correlated with the levels of FBW7 and a poor prognosis in patients with human carcinoma. In summary, we found that PRMT5 functions as a target for improving cancer therapy efficacy, by acting to reduce the counteraction of ferroptosis by tumour cells by means of PRMT5-enhanced GPX4 stability.
format Artículo científico
id pubmed_40033101
institution PubMed
language en
publishDate 2025
publisher Nature cell biology
record_format pubmed
spellingShingle PRMT5-mediated arginine methylation stabilizes GPX4 to suppress ferroptosis in cancer.
Fan, Yizeng
Wang, Yuzhao
Dan, Weichao
Zhang, Yilei
Nie, Li
Ma, Zhiqiang
Zhuang, Yanxin
Liu, Bo
Li, Mengxing
Liu, Tianjie
Wang, Zixi
Ye, Leihong
Wei, Yi
Lei, Yuzeshi
Guo, Chendong
An, Jiale
Wang, Chi
Zhang, Yulin
Zeng, Jin
Wei, Wenyi
Gan, Boyi
Li, Lei
Ferroptosis
Protein-Arginine N-Methyltransferases
Humans
Animals
Phospholipid Hydroperoxide Glutathione Peroxidase
Methylation
Arginine
Mice
Neoplasms
F-Box-WD Repeat-Containing Protein 7
Cell Line, Tumor
Female
Ubiquitination
Mice, Nude
Mice, Inbred BALB C
HEK293 Cells
PRMT5-mediated arginine methylation stabilizes GPX4 to suppress ferroptosis in cancer. Fan, Yizeng Wang, Yuzhao Dan, Weichao Zhang, Yilei Nie, Li Ma, Zhiqiang Zhuang, Yanxin Liu, Bo Li, Mengxing Liu, Tianjie Wang, Zixi Ye, Leihong Wei, Yi Lei, Yuzeshi Guo, Chendong An, Jiale Wang, Chi Zhang, Yulin Zeng, Jin Wei, Wenyi Gan, Boyi Li, Lei Ferroptosis Protein-Arginine N-Methyltransferases Humans Animals Phospholipid Hydroperoxide Glutathione Peroxidase Methylation Arginine Mice Neoplasms F-Box-WD Repeat-Containing Protein 7 Cell Line, Tumor Female Ubiquitination Mice, Nude Mice, Inbred BALB C HEK293 Cells The activation of ferroptosis has shown great potential for cancer therapy from an unconventional perspective, but revealing the mechanisms underlying the suppression of tumour-intrinsic ferroptosis to promote tumorigenesis remains a challenging task. Here we report that methionine is metabolized into S-adenosylmethionine, which functions as a methyl-group donor to trigger symmetric dimethylation of glutathione peroxidase 4 (GPX4) at the conserved arginine 152 (R152) residue, along with a prolonged GPX4 half-life. Inhibition of protein arginine methyltransferase 5 (PRMT5), which catalyses GPX4 methylation, decreases GPX4 protein levels by impeding GPX4 methylation and increasing ferroptosis inducer sensitivity in vitro and in vivo. This methylation prevents Cullin1-FBW7 E3 ligase binding to GPX4, thereby abrogating the ubiquitination-mediated GPX4 degradation. Notably, combining PRMT5 inhibitor treatment with ferroptotic therapies markedly suppresses tumour progression in mouse tumour models. In addition, the levels of GPX4 are negatively correlated with the levels of FBW7 and a poor prognosis in patients with human carcinoma. In summary, we found that PRMT5 functions as a target for improving cancer therapy efficacy, by acting to reduce the counteraction of ferroptosis by tumour cells by means of PRMT5-enhanced GPX4 stability.
title PRMT5-mediated arginine methylation stabilizes GPX4 to suppress ferroptosis in cancer.
topic Ferroptosis
Protein-Arginine N-Methyltransferases
Humans
Animals
Phospholipid Hydroperoxide Glutathione Peroxidase
Methylation
Arginine
Mice
Neoplasms
F-Box-WD Repeat-Containing Protein 7
Cell Line, Tumor
Female
Ubiquitination
Mice, Nude
Mice, Inbred BALB C
HEK293 Cells
url https://pubmed.ncbi.nlm.nih.gov/40033101/