Evidence map›Paper›PMID 40830268›Full record

ReviewNature reviews. Molecular cell biology2026

Biochemistry and regulation of histone lysine L-lactylation.

Xinlei Sheng, Hening Lin, Philip A Cole, Yingming Zhao

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed, 1 pooled it
–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

64 citing papers in PubMed, 1 synthesis or guideline pooled it.

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4 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

4 authors.

Xinlei ShengThe Ben May Department for Cancer Research, The University of Chicago, Chicago, IL, USA.
Hening LinHoward Hughes Medical Institute, Department of Medicine, The University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-0255-2701
Philip A ColeDivision of Genetics, Department of Medicine, Brigham and Women's Hospital, Boston, MA, USA.ORCID http://orcid.org/0000-0001-6873-7824
Yingming ZhaoThe Ben May Department for Cancer Research, The University of Chicago, Chicago, IL, USA. yzhao2@bsd.uchicago.edu.ORCID http://orcid.org/0000-0003-1928-2151

Funding

Protein Acylation and Methylation Mechanisms_Administrative SupplementR37GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2013 to 2022
$4.1M
Histone lactylation pathway in hair cycle: deacylases and their protein targetsR01AR078555 · NIAMS · UNIVERSITY OF CHICAGO · PI LIN, HENING, ZHAO, YINGMING · 2021 to 2025
$3.3M
Lactate production by tumor associated macrophages promotes tumorigenesisR01CA251677 · NCI · UNIVERSITY OF CHICAGO · PI BECKER, LEV, ZHAO, YINGMING · 2021 to 2025
$2.8M
Chemical Approaches to Understanding Reversible Lysine ModificationsR35GM149229 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI PHILIP A COLE · 2023 to 2026
$1.9M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA251677NIAMS NIH HHS R01 AR078555NIGMS NIH HHS R35 GM149229NIGMS NIH HHS R37 GM062437
6 · The paper itself

Abstract

Histone L-lactylation is a newly identified, metabolism-linked short-chain Lys acylation. Mounting evidence indicates that Lys L-lactylation has key roles in transcription regulation and many other cellular processes and is associated with diverse pathophysiological changes. In this Review, we discuss the unique features of histone L-lactylation, emphasizing the differences between L-lactylation and its isomers, such as D-lactylation. We discuss the regulation of L-lactylation by writers and erasers, its readers and its cofactor L-lactyl-CoA. We highlight the dynamic regulation of nuclear L-lactyl-CoA and L-lactyl-CoA synthetases, which are crucial determinants of the specificity of histone Lys L-lactylation. We also discuss an emerging L-lactyl-CoA-independent L-lactylation pathway. By integrating these findings, we aim to deepen our understanding of the biochemistry and regulation of histone L-lactylation and its broad biological significance.

Indexed as

HistonesLysineAcylationAnimalsCoenzyme A LigasesHumansProtein Processing, Post-TranslationalCoenzyme A LigasesHistonesLysine

Identifiers

PMID40830268
PMCPMC12920031

What OpenQuestion holds

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Registered trials

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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.