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Cell Death & Disease

Cell Death & Disease

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Deacetylation of TALDO1 by HDAC6 promotes glycolysis and nasopharyngeal carcinoma progression through a moonlighting function

Published:21 October 2025 DOI: 10.1038/s41419-025-08057-2 PMID: 41120289
Xingzhi Peng,?Peijun Zhou,?Kun Zhang,?Likang Chen,?Min Tang,?Qin Zhou,?Jinwu Peng,?Lifang Yang

Abstract

Aberrant metabolic enzymes drive glucose metabolism reprogramming, which plays a crucial role in tumor malignancy and metastasis. Protein acetylation is one of the key regulatory mechanisms of metabolic enzyme function, yet its precise role requires further clarification. In the present study, we reported that the deacetylation and low expression of transaldolase 1 (TALDO1) mediated by HDAC6 weakened the inhibitory effect of TALDO1 on tumor proliferation and metastasis in nasopharyngeal carcinoma (NPC). Mechanistically, highly expressed HDAC6 induced lysine 7 (K7) deacetylation of TALDO1, which could inhibit SMURF1-mediated K63-linked ubiquitination, thus reducing the protein stability of TALDO1. Notably, TALDO1 deacetylation inhibited its nuclear translocation and interaction with BRCA1, thereby reducing the inhibition of c-Myc transcriptional activation, promoting the expression of HK2/LDHA/PDK1, and further enhancing glycolysis independent of TALDO1 enzyme activity. This research elucidated the regulatory mechanism of TALDO1 from the perspective of acetylation modification, clarified the moonlighting functions of TALDO1 in metabolic reprogramming, and provided novel biomarkers and intervention strategies, such as HDAC inhibitors, for the clinical treatment of NPC.

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