TACC3 enhances glycolysis in bladder cancer cells through inducing acetylation of c-Myc

Abstract The proliferation of bladder cancer (BC) cells is driven by metabolic reprogramming, marked by a glycolytic dependency to sustain uncontrolled growth. While Transforming Acidic Coiled-Coil Containing Protein 3 (TACC3) is known to promote BC progression and correlate with poor prognosis, the...

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Main Authors: Zhirui Lin, Falian Liang, Gengde Hong, Xizhen Jiang, Qingling Zhang, Mengyao Wang
Format: Article
Language:English
Published: Nature Publishing Group 2025-04-01
Series:Cell Death and Disease
Online Access:https://doi.org/10.1038/s41419-025-07645-6
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author Zhirui Lin
Falian Liang
Gengde Hong
Xizhen Jiang
Qingling Zhang
Mengyao Wang
author_facet Zhirui Lin
Falian Liang
Gengde Hong
Xizhen Jiang
Qingling Zhang
Mengyao Wang
author_sort Zhirui Lin
collection DOAJ
description Abstract The proliferation of bladder cancer (BC) cells is driven by metabolic reprogramming, marked by a glycolytic dependency to sustain uncontrolled growth. While Transforming Acidic Coiled-Coil Containing Protein 3 (TACC3) is known to promote BC progression and correlate with poor prognosis, the mechanisms underlying its upregulation and role in aerobic glycolysis remain unclear. Here, we identify E2F3 as a direct transcriptional activator of TACC3, with its amplification in BC driving elevated TACC3 expression. TACC3 overexpression enhances glycolysis, increasing glucose consumption, lactate production, and expression of glycolytic enzymes (e.g., GLUT1, HK2, PFKFB3), while its knockdown suppresses these effects. Pharmacological inhibition of glycolysis abrogates TACC3-driven tumor growth in vitro and in vivo. Mechanistically, TACC3 interacts with c-Myc, promoting its acetylation at lysine 323 (K323) by recruiting the acetyltransferase PCAF and antagonizing the deacetylase SIRT1. This acetylation stabilizes c-Myc, amplifying its transcriptional activation of glycolytic targets. Our findings establish TACC3 as a critical regulator of c-Myc-driven metabolic reprogramming in BC, highlighting its potential as a therapeutic target to disrupt glycolysis and oncogenic c-Myc signaling.
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publishDate 2025-04-01
publisher Nature Publishing Group
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series Cell Death and Disease
spelling doaj-art-db3f3a8899ea418b850b3a0a1b508ddb2025-08-20T03:18:42ZengNature Publishing GroupCell Death and Disease2041-48892025-04-0116111210.1038/s41419-025-07645-6TACC3 enhances glycolysis in bladder cancer cells through inducing acetylation of c-MycZhirui Lin0Falian Liang1Gengde Hong2Xizhen Jiang3Qingling Zhang4Mengyao Wang5Institute of Medical Research, Guangdong Provincial People’s Hospital (Guangdong Academy of Medical Sciences), Southern Medical UniversityRadiation Oncology Department, Guangzhou Institute of Cancer Research, the Affiliated Cancer Hospital, Guangzhou Medical UniversityRadiation Oncology Department, Guangzhou Institute of Cancer Research, the Affiliated Cancer Hospital, Guangzhou Medical UniversityRadiation Oncology Department, Guangzhou Institute of Cancer Research, the Affiliated Cancer Hospital, Guangzhou Medical UniversityDepartment of Pathology, Guangdong Provincial People’s Hospital (Guangdong Academy of Medical Sciences), Southern Medical UniversityRadiation Oncology Department, Guangzhou Institute of Cancer Research, the Affiliated Cancer Hospital, Guangzhou Medical UniversityAbstract The proliferation of bladder cancer (BC) cells is driven by metabolic reprogramming, marked by a glycolytic dependency to sustain uncontrolled growth. While Transforming Acidic Coiled-Coil Containing Protein 3 (TACC3) is known to promote BC progression and correlate with poor prognosis, the mechanisms underlying its upregulation and role in aerobic glycolysis remain unclear. Here, we identify E2F3 as a direct transcriptional activator of TACC3, with its amplification in BC driving elevated TACC3 expression. TACC3 overexpression enhances glycolysis, increasing glucose consumption, lactate production, and expression of glycolytic enzymes (e.g., GLUT1, HK2, PFKFB3), while its knockdown suppresses these effects. Pharmacological inhibition of glycolysis abrogates TACC3-driven tumor growth in vitro and in vivo. Mechanistically, TACC3 interacts with c-Myc, promoting its acetylation at lysine 323 (K323) by recruiting the acetyltransferase PCAF and antagonizing the deacetylase SIRT1. This acetylation stabilizes c-Myc, amplifying its transcriptional activation of glycolytic targets. Our findings establish TACC3 as a critical regulator of c-Myc-driven metabolic reprogramming in BC, highlighting its potential as a therapeutic target to disrupt glycolysis and oncogenic c-Myc signaling.https://doi.org/10.1038/s41419-025-07645-6
spellingShingle Zhirui Lin
Falian Liang
Gengde Hong
Xizhen Jiang
Qingling Zhang
Mengyao Wang
TACC3 enhances glycolysis in bladder cancer cells through inducing acetylation of c-Myc
Cell Death and Disease
title TACC3 enhances glycolysis in bladder cancer cells through inducing acetylation of c-Myc
title_full TACC3 enhances glycolysis in bladder cancer cells through inducing acetylation of c-Myc
title_fullStr TACC3 enhances glycolysis in bladder cancer cells through inducing acetylation of c-Myc
title_full_unstemmed TACC3 enhances glycolysis in bladder cancer cells through inducing acetylation of c-Myc
title_short TACC3 enhances glycolysis in bladder cancer cells through inducing acetylation of c-Myc
title_sort tacc3 enhances glycolysis in bladder cancer cells through inducing acetylation of c myc
url https://doi.org/10.1038/s41419-025-07645-6
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