Evidence map›Paper›PMID 39333081›Full record

ArticleNature communications2024

Metabolic regulation of cytoskeleton functions by HDAC6-catalyzed α-tubulin lactylation.

Shuangshuang Sun, Zhe Xu, Liying He, Yihui Shen, Yuqing Yan, Xubing Lv, Xujing Zhu, Wei Li, Wei-Ya Tian, Yongjun Zheng and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

79 citing papers in PubMed.

  1. Review
  2. The histone deacetylase family in health and disease.Signal transduction and targeted therapy · 2026
    Review
  3. Review
  4. Lactylation Modification and Esophageal Cancer: Research Progress From Hypoxia-Induced Metabolic Reprogramming to Immune Escape.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  5. Review
  6. Review
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  12. Review
  13. Review
  14. Article
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  18. Article
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  20. Review

19 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Shuangshuang Sun *School of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Zhe Xu *School of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Liying HeSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Yihui ShenSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Yuqing YanDepartment of Pain management, HuaDong Hospital Affiliated to Fudan University, Shanghai, China.
Xubing LvSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Xujing ZhuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Wei LiSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Wei-Ya TianSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Yongjun ZhengDepartment of Pain management, HuaDong Hospital Affiliated to Fudan University, Shanghai, China.
Sen LinDepartment of Neurology, 2nd Affiliated Hospital, Army Medical University, Chongqing, China.
Yadong SunSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.ORCID 0000-0003-4470-6630
Lei LiSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China. lilei@shanghaitech.edu.cn.ORCID 0000-0002-9542-4767

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31871044National Natural Science Foundation of China (National Science Foundation of China) 91949117
6 · The paper itself

Abstract

Posttranslational modifications (PTMs) of tubulin, termed the "tubulin code", play important roles in regulating microtubule functions within subcellular compartments for specialized cellular activities. While numerous tubulin PTMs have been identified, a comprehensive understanding of the complete repertoire is still underway. In this study, we report that α-tubulin lactylation is catalyzed by HDAC6 by using lactate to increase microtubule dynamics in neurons. We identify lactylation on lysine 40 of α-tubulin in the soluble tubulin dimers. Notably, lactylated α-tubulin enhances microtubule dynamics and facilitates neurite outgrowth and branching in cultured hippocampal neurons. Moreover, we discover an unexpected function of HDAC6, acting as the primary lactyltransferase to catalyze α-tubulin lactylation. HDAC6-catalyzed lactylation is a reversible process, dependent on lactate concentrations. Intracellular lactate concentration triggers HDAC6 to lactylate α-tubulin, a process dependent on its deacetylase activity. Additionally, the lactyltransferase activity may be conserved in HDAC family proteins. Our study reveals the primary role of HDAC6 in regulating α-tubulin lactylation, establishing a link between cell metabolism and cytoskeleton functions.

Indexed as

CytoskeletonHistone Deacetylase 6MicrotubulesNeuronsProtein Processing, Post-TranslationalTubulinAnimalsCells, CulturedHippocampusHumansLactic AcidLysineMiceNeuronal OutgrowthRatsHDAC6 protein, humanHdac6 protein, mouseHistone Deacetylase 6Lactic AcidLysineTubulin

Identifiers

PMID39333081
PMCPMC11437170

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.