干细胞
生物
HMOX1型
细胞生物学
髓系白血病
血红素
白血病
血红素加氧酶
生物化学
癌症研究
造血
核孔蛋白
化学
下调和上调
分解代谢
造血干细胞
脂质过氧化
转录因子
疏孔素原脱氨酶
细胞保护
髓样
分子生物学
作者
Zhe Chen,Feng Wu,Wei Zhang,Wei Guo,Yan Li,Qiang Gong,Yue Wei,Linfeng Li,Tao Chen,Xueya Zhao,Jianwen Xiao,Hanqing Zeng,Jianchuan Deng,Huabing Li,Li Wang,Zufeng Guo,Yu Hou
出处
期刊:Blood
[Elsevier BV]
日期:2026-08-25
标识
DOI:10.1182/blood.2026033244
摘要
Chromosomal translocations involving nucleoporin (NUP) loci, such as NUP98 and NUP214, are recurrent in acute myeloid leukemia (AML). However, the intrinsic functions of wild-type nucleoporins in AML remain largely unknown. By screening the NUP family, we identified NUP214 as a frequently overexpressed gene and a critical fitness determinant in leukemia stem cells (LSCs). NUP214 acts as a conserved driver of LSC survival by restricting heme catabolism, limiting Fe²⁺ accumulation, and suppressing lipid peroxidation. Conversely, NUP214 deficiency leads to upregulation of heme oxygenase 1 (HMOX1) and arachidonate 15-lipoxygenase (ALOX15), causing heme exhaustion and excessive lipid peroxidation, which ultimately triggers ferroptosis in LSCs and impairs AML progression. Mechanistically, NUP214 translocates into the nucleoplasm where it blocks Sub1-mediated RNA polymerase II recruitment to repress transcription of the key pro-ferroptotic genes HMOX1 and ALOX15, revealing a non-canonical role beyond its nuclear pore function. Furthermore, we developed the small-molecule compound 0449-b, which acts as a selective NUP214 degrader by recruiting NUP214 to the Cullin5-Rbx2 E3 ligase complex, inducing its neddylation and proteasomal degradation. 0449-b potently triggers LSC ferroptosis and exhibits anti-leukemic activity in vivo, while sparing normal hematopoietic stem cells. Collectively, our findings establish NUP214 as a critical oncoprotein that orchestrates heme metabolism and lipid peroxidation to sustain LSCs, and highlight NUP214-targeted degradation as a promising intervention strategy for AML.
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