Evidence map›Paper›PMID 38773107›Full record

ArticleNature communications2024

The SUN-family protein Sad1 mediates heterochromatin spatial organization through interaction with histone H2A-H2B.

Wenqi Sun, Qianhua Dong, Xueqing Li, Jinxin Gao, Xianwen Ye, Chunyi Hu, Fei Li, Yong Chen

Abstract read
PubMed Full text at PMC Publisher
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 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

8 authors.

Wenqi Sun *State Key Laboratory of Molecular Biology, Key Laboratory of Epigenetic Regulation and Intervention, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, China.
Qianhua Dong *Department of Biology, New York University, New York, NY, USA.
Xueqing Li *State Key Laboratory of Molecular Biology, Key Laboratory of Epigenetic Regulation and Intervention, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, China.
Jinxin Gao *Department of Biology, New York University, New York, NY, USA.
Xianwen YeUniversity of Chinese Academy of Sciences, Beijing, China.
Chunyi HuDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore.ORCID http://orcid.org/0000-0003-4509-4840
Fei LiDepartment of Biology, New York University, New York, NY, USA. fl43@nyu.edu.ORCID http://orcid.org/0000-0002-1206-9684
Yong ChenState Key Laboratory of Molecular Biology, Key Laboratory of Epigenetic Regulation and Intervention, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, China. yongchen@sibcb.ac.cn.ORCID http://orcid.org/0000-0001-5857-6086

Funding

Molecular Basis of Centromere Specification and InheritanceR35GM134920 · NIGMS · NEW YORK UNIVERSITY · PI LI, FEI · 2020 to 2025
$4.2M
National Natural Science Foundation of China (National Science Foundation of China) 31970576NIGMS NIH HHS R35 GM134920
6 · The paper itself

Abstract

Heterochromatin is generally associated with the nuclear periphery, but how the spatial organization of heterochromatin is regulated to ensure epigenetic silencing remains unclear. Here we found that Sad1, an inner nuclear membrane SUN-family protein in fission yeast, interacts with histone H2A-H2B but not H3-H4. We solved the crystal structure of the histone binding motif (HBM) of Sad1 in complex with H2A-H2B, revealing the intimate contacts between Sad1

Indexed as

HeterochromatinHistonesProtein BindingSchizosaccharomycesSchizosaccharomyces pombe ProteinsCell Cycle ProteinsCrystallography, X-RayHistone DeacetylasesNuclear EnvelopeNuclear ProteinsTelomereCell Cycle ProteinsClr3 protein, S pombeHeterochromatinHistone DeacetylasesHistonesNuclear ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID38773107
PMCPMC11109203

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

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 Socratic graph.