Evidence map›Paper›PMID 30100181›Full record

ArticleCell2018

Crystal Structure of the COMPASS H3K4 Methyltransferase Catalytic Module.

Peter L Hsu, Heng Li, Ho-Tak Lau, Calvin Leonen, Abhinav Dhall, Shao-En Ong, Champak Chatterjee, Ning Zheng

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

58 citing papers in PubMed, 99 citations in OpenAlex.

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  11. The FBXW7-KMT2 axis in cancer-associated fibroblasts controls tumor growth via an epigenetic-paracrine mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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 at 2 institutions in 1 country.

Peter L HsuDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Heng LiDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Ho-Tak LauDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Calvin LeonenDepartment of Chemistry, University of Washington, Seattle, WA 98195, USA.
Abhinav DhallDepartment of Chemistry, University of Washington, Seattle, WA 98195, USA.
Shao-En OngDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Champak ChatterjeeDepartment of Chemistry, University of Washington, Seattle, WA 98195, USA.
Ning ZhengDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA; Howard Hughes Medical Institute, Box 357280, Seattle, WA 98125, USA. Electronic address: nzheng@uw.edu.
University of Washington · USHoward Hughes Medical Institute · US

Funding

TRAINING IN MOLECULAR BIOPHYSICST32GM008268 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M, ZHENG, NING · 1988 to 2023
$8.6M
Chemical Strategies to Investigate Gene Regulation By Histone SumoylationR01GM110430 · NIGMS · UNIVERSITY OF WASHINGTON · PI CHATTERJEE, CHAMPAK · 2014 to 2022
$2.5M
Structure and Mechanism of the SET1/COMPASS H3K4 Methyltransferase ComplexR01HD097408 · NICHD · UNIVERSITY OF WASHINGTON · PI CHATTERJEE, CHAMPAK, ZHENG, NING · 2020 to 2024
$1.9M
Characterizing Muscle Regulatory Elements with Mass Spectrometry-Based ProteomicsR01AR065459 · NIAMS · UNIVERSITY OF WASHINGTON · PI ONG, SHAO-EN · 2013 to 2017
$1.6M
Howard Hughes Medical InstituteNIAMS NIH HHS R01 AR065459NICHD NIH HHS R01 HD097408NIGMS NIH HHS R01 GM110430NIGMS NIH HHS T32 GM008268
6 · The paper itself

Abstract

The SET1/MLL family of histone methyltransferases is conserved in eukaryotes and regulates transcription by catalyzing histone H3K4 mono-, di-, and tri-methylation. These enzymes form a common five-subunit catalytic core whose assembly is critical for their basal and regulated enzymatic activities through unknown mechanisms. Here, we present the crystal structure of the intact yeast COMPASS histone methyltransferase catalytic module consisting of Swd1, Swd3, Bre2, Sdc1, and Set1. The complex is organized by Swd1, whose conserved C-terminal tail not only nucleates Swd3 and a Bre2-Sdc1 subcomplex, but also joins Set1 to construct a regulatory pocket next to the catalytic site. This inter-subunit pocket is targeted by a previously unrecognized enzyme-modulating motif in Swd3 and features a doorstop-style mechanism dictating substrate selectivity among SET1/MLL family members. By spatially mapping the functional components of COMPASS, our results provide a structural framework for understanding the multifaceted functions and regulation of the H3K4 methyltransferase family.

Indexed as

Amino Acid SequenceAnimalsCatalytic DomainCell LineCrystallography, X-RayDNA-Binding ProteinsFungal ProteinsHistone-Lysine N-MethyltransferaseHistonesHumansInsectaKluyveromycesMethylationNuclear ProteinsProtein DomainsSaccharomyces cerevisiaeASH2L protein, humanDNA-Binding ProteinsFungal ProteinsHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiaeTranscription FactorschromatinCOMPASSepigeneticsH3K4 methylationmethyltransferasesMLLSet1structural biology

Identifiers

PMID30100181
PMCPMC6108940
OpenAlexW2886836393

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.