Evidence map›Paper›PMID 36351927›Full record

ArticleNature communications2022

CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site.

Lihu Gong, Xiuli Liu, Lianying Jiao, Xin Yang, Andrew Lemoff, Xin Liu

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. BiallelicInternational journal of molecular sciences · 2026
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  3. Review
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  7. CXCR5Nature communications · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. CBX2 suppresses interferon signaling to diminish tumor immunogenicity via a noncanonical corepressor complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Article
  20. 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

6 authors at 2 institutions in 2 countries.

Lihu Gong *Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA.ORCID 0000-0001-5482-2120
Xiuli Liu *Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA.
Lianying Jiao *Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA.
Xin YangCecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA.
Andrew LemoffDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA.ORCID 0000-0002-4943-0170
Xin LiuCecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, TX, 75390, USA. xin.liu@utsouthwestern.edu.ORCID 0000-0002-5646-423X
The University of Texas Southwestern Medical Center · USSouthwestern Medical Center · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Molecular Basis of Gene Regulation by Polycomb Repressive Complex 2R35GM136308 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LIU, XIN · 2020 to 2024
$2.9M
Structural Basis of Gene Regulation by Polycomb Repressive Complex 2R01GM121662 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LIU, XIN · 2017 to 2020
$1.3M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM121662NIGMS NIH HHS R35 GM136308
6 · The paper itself

Abstract

Polycomb repressive complex 2 (PRC2) plays a key role in maintaining cell identity during differentiation. Methyltransferase activity of PRC2 on histone H3 lysine 27 is regulated by diverse cellular mechanisms, including posttranslational modification. Here, we report a unique phosphorylation-dependent mechanism stimulating PRC2 enzymatic activity. Residue S583 of SUZ12 is phosphorylated by casein kinase 2 (CK2) in cells. A crystal structure captures phosphorylation in action: the flexible phosphorylation-dependent stimulation loop harboring S583 becomes engaged with the catalytic SET domain through a phosphoserine-centered interaction network, stabilizing the enzyme active site and in particular S-adenosyl-methionine (SAM)-binding pocket. CK2-mediated S583 phosphorylation promotes catalysis by enhancing PRC2 binding to SAM and nucleosomal substrates and facilitates reporter gene repression. Loss of S583 phosphorylation impedes PRC2 recruitment and H3K27me3 deposition in pluripotent mESCs and compromises the ability of PRC2 to maintain differentiated cell identity.

Indexed as

Casein Kinase IIPolycomb Repressive Complex 2Catalytic DomainHistonesPhosphorylationCasein Kinase IIHistonesPolycomb Repressive Complex 2

Identifiers

PMID36351927
PMCPMC9645763
OpenAlexW4308627630

What OpenQuestion 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 OpenQuestion graph.