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The GCN5L2-SIX1 complex drives glycolysis to promote progression of triple-negative breast cancer.

Yuning Liao, Shusha Yin, E-Ying Peng, Jinjie Wu, Yu Yao, Wanying He, Hongbiao Huang, Qing Liu, Yuanfei Deng, Leyi Yao, Gengxi Cai

Cancer lettersOct 28, 2026PMID 42601012doi:10.1016/j.canlet.2026.218770 Journal ArticlepubmedProvenance
Source
PubMed
Retrieved
Sep 13, 2026
Layer
normalized (units and labels harmonized; values unchanged)
Run
ING-PUBMED-20260913-000001
Published

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Lactylation, a lactate-dependent posttranslational modification, is involved in cancer development. Here, we showed that GCN5L2 physically interacts with nuclear SIX1 and acts as a key regulator of SIX1 lactylation. GCN5L2 depletion promotes APC/Cdh1 binding to SIX1, increases SIX1 ubiquitination,…

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