Evidence map›Paper›PMID 20541251›Full record

ArticleCell2010

Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression.

Zhanxin Wang, Jikui Song, Thomas A Milne, Gang G Wang, Haitao Li, C David Allis, Dinshaw J Patel

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

120 citing papers in PubMed, 205 citations in OpenAlex.

  1. Review
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  5. Review
  6. Review
  7. Article
  8. Assessing the functional roles of coevolving PHD finger residues.Protein science : a publication of the Protein Society · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Non-histone binding functions of PHD fingers.Trends in biochemical sciences · 2023
    Review
  18. Article
  19. Article
  20. Article

60 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Zhanxin WangStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Jikui Song
Thomas A Milne
Gang G Wang
Haitao Li
C David Allis
Dinshaw J Patel
Memorial Sloan Kettering Cancer Center · USRockefeller University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Cancer epigenetics: Understanding histone methylation in leukemia stem cellsK99CA151683 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WANG, G GREG · 2010 to 2011
$276k
NCI NIH HHS K99 CA151683NCI NIH HHS P30 CA008748
6 · The paper itself

Abstract

The MLL1 gene is a frequent target for recurrent chromosomal translocations, resulting in transformation of hematopoietic precursors into leukemia stem cells. Here, we report on structure-function studies that elucidate molecular events in MLL1 binding of histone H3K4me3/2 marks and recruitment of the cyclophilin CyP33. CyP33 contains a PPIase and a RRM domain and regulates MLL1 function through HDAC recruitment. We find that the PPIase domain of CyP33 regulates the conformation of MLL1 through proline isomerization within the PHD3-Bromo linker, thereby disrupting the PHD3-Bromo interface and facilitating binding of the MLL1-PHD3 domain to the CyP33-RRM domain. H3K4me3/2 and CyP33-RRM target different surfaces of MLL1-PHD3 and can bind simultaneously to form a ternary complex. Furthermore, the MLL1-CyP33 interaction is required for repression of HOXA9 and HOXC8 genes in vivo. Our results highlight the role of PHD3-Bromo cassette as a regulatory platform, orchestrating MLL1 binding of H3K4me3/2 marks and cyclophilin-mediated repression through HDAC recruitment.

Indexed as

Amino Acid SequenceCell LineCrystallography, X-RayCyclophilinsHistone DeacetylasesHistone-Lysine N-MethyltransferaseHistonesHumansMethylationModels, MolecularMolecular Sequence DataMyeloid-Lymphoid Leukemia ProteinNuclear Magnetic Resonance, BiomolecularProlineProtein Interaction Domains and MotifsCyclophilinsHistone DeacetylasesHistone-Lysine N-MethyltransferaseHistonesKMT2A protein, humanMyeloid-Lymphoid Leukemia ProteinPPIE protein, humanProline

Identifiers

PMID20541251
PMCPMC4690531
OpenAlexW2058001379

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.