Evidence map›Paper›PMID 27775714›Full record

ArticleNature chemical biology2016

Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2.

Xiaozhe Xiong, Tatyana Panchenko, Shuang Yang, Shuai Zhao, Peiqiang Yan, Wenhao Zhang, Wei Xie, Yuanyuan Li, Yingming Zhao, C David Allis and 1 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
8.7field-weighted citation impact, top 2% of its field
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

119 citing papers in PubMed, 181 citations in OpenAlex.

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  14. Integrative multiomics elucidate crotonylation-associated GCDH in Parkinson's disease pathogenesis via metabolome remodeling.Mammalian genome : official journal of the International Mammalian Genome Society · 2025
    Article
  15. Review
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  18. Histone crotonylation in tumors (Review).Molecular and clinical oncology · 2025
    Review
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59 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

11 authors at 5 institutions in 2 countries.

Xiaozhe XiongMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Tatyana PanchenkoLaboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, New York, USA.
Shuang YangMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Shuai ZhaoMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Peiqiang YanMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Wenhao ZhangSchool of Life Sciences, Tsinghua University, Beijing, China.
Wei XieSchool of Life Sciences, Tsinghua University, Beijing, China.
Yuanyuan LiMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Yingming ZhaoBen May Department of Cancer Research, The University of Chicago, Chicago, Illinois, USA.
C David AllisLaboratory of Chromatin Biology and Epigenetics, The Rockefeller University, New York, New York, USA.
Haitao LiMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0002-6686-1677
Tsinghua University · CNCenter for Life Sciences · CNRockefeller University · USSichuan University · CNUniversity of Chicago · US

Funding

INFLUENCE OF HISTONE H1 AND HMGS ON GENE EXPRESSIONR01GM040922 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI ALLIS, CHARLES DAVID · 1989 to 2022
$10.0M
Functional and Mechanistic Study of Histone Crotonylation in Hematological MalignanciesR01CA204639 · NCI · ROCKEFELLER UNIVERSITY · PI ALLIS, CHARLES DAVID, ARMSTRONG, SCOTT A · 2016 to 2020
$3.5M
SIRT6 and lysine fatty acylation in macrophage inflammationR01DK107868 · NIDDK · CORNELL UNIVERSITY · PI LIN, HENING, ZHAO, YINGMING · 2016 to 2019
$2.0M
Systems-wide analysis of histone lysine 2-hydroxyisobutyrylation pathwayR01GM115961 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHAO, YINGMING · 2016 to 2019
$1.8M
Biochemistry of lysine crotonylation pathwayR01GM105933 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHAO, YINGMING · 2013 to 2016
$1.7M
Mechanism for Chromatin Accessibility through a Novel Histone PhosphorylationF32GM112365 · NIGMS · ROCKEFELLER UNIVERSITY · PI PANCHENKO, TATYANA · 2015 to 2016
$77k
NCI NIH HHS R01 CA204639NIDDK NIH HHS R01 DK107868NIGMS NIH HHS F32 GM112365NIGMS NIH HHS R01 GM040922NIGMS NIH HHS R01 GM105933NIGMS NIH HHS R01 GM115961
6 · The paper itself

Abstract

Recognition of histone covalent modifications by 'reader' modules constitutes a major mechanism for epigenetic regulation. A recent upsurge of newly discovered histone lysine acylations, such as crotonylation (Kcr), butyrylation (Kbu), and propionylation (Kpr), greatly expands the coding potential of histone lysine modifications. Here we demonstrate that the histone acetylation-binding double PHD finger (DPF) domains of human MOZ (also known as KAT6A) and DPF2 (also known as BAF45d) accommodate a wide range of histone lysine acylations with the strongest preference for Kcr. Crystal structures of the DPF domain of MOZ in complex with H3K14cr, H3K14bu, and H3K14pr peptides reveal that these non-acetyl acylations are anchored in a hydrophobic 'dead-end' pocket with selectivity for crotonylation arising from intimate encapsulation and an amide-sensing hydrogen bonding network. Immunofluorescence and chromatin immunoprecipitation (ChIP)-quantitative PCR (qPCR) showed that MOZ and H3K14cr colocalize in a DPF-dependent manner. Our studies call attention to a new regulatory mechanism centered on histone crotonylation readout by DPF family members.

Indexed as

Protein Interaction Domains and MotifsAcetylationDNA-Binding ProteinsHistone AcetyltransferasesHistonesHumansTranscription FactorsDNA-Binding ProteinsDPF2 protein, humanHistone AcetyltransferasesHistonesKAT6A protein, humanTranscription Factors

Identifiers

PMID27775714
PMCPMC5253430
OpenAlexW2535463226

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.