Evidence map›Paper›PMID 15199122›Full record

ArticleMolecular and cellular biology2004

Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression.

Akihiko Yokoyama, Zhong Wang, Joanna Wysocka, Mrinmoy Sanyal, Deborah J Aufiero, Issay Kitabayashi, Winship Herr, Michael L Cleary

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 372 papers.

0numbers the graph read from it
0cells of the map it votes in
372citing papers in PubMed
14.9field-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

372 citing papers in PubMed, 642 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Menin in Cancer.Genes · 2024
    Review
  20. HBO1, a MYSTerious KAT and its links to cancer.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review

312 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

8 authors at 2 institutions in 1 country.

Akihiko YokoyamaDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Zhong Wang
Joanna Wysocka
Mrinmoy Sanyal
Deborah J Aufiero
Issay Kitabayashi
Winship Herr
Michael L Cleary
Stanford University · USCold Spring Harbor Laboratory · US

Funding

VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI William Richard McCombie · 1985 to 2026
$116.8M
PATHOLOGY AND BIOLOGY OF LEUKEMIA ONCOGENESR01CA055029 · NCI · STANFORD UNIVERSITY · PI CLEARY, MICHAEL L · 1991 to 2008
$3.1M
CELLULAR FUNCTIONS OF HCFR01GM054598 · NIGMS · COLD SPRING HARBOR LABORATORY · PI MYERS, MICHAEL P · 1996 to 2005
$1.2M
NCI NIH HHS CA13106NCI NIH HHS CA55029NCI NIH HHS P01 CA013106NCI NIH HHS R01 CA055029NIGMS NIH HHS GM54598NIGMS NIH HHS R01 GM054598
6 · The paper itself

Abstract

MLL (for mixed-lineage leukemia) is a proto-oncogene that is mutated in a variety of human leukemias. Its product, a homolog of Drosophila melanogaster trithorax, displays intrinsic histone methyltransferase activity and functions genetically to maintain embryonic Hox gene expression. Here we report the biochemical purification of MLL and demonstrate that it associates with a cohort of proteins shared with the yeast and human SET1 histone methyltransferase complexes, including a homolog of Ash2, another Trx-G group protein. Two other members of the novel MLL complex identified here are host cell factor 1 (HCF-1), a transcriptional coregulator, and the related HCF-2, both of which specifically interact with a conserved binding motif in the MLL(N) (p300) subunit of MLL and provide a potential mechanism for regulating its antagonistic transcriptional properties. Menin, a product of the MEN1 tumor suppressor gene, is also a component of the 1-MDa MLL complex. Abrogation of menin expression phenocopies loss of MLL and reveals a critical role for menin in the maintenance of Hox gene expression. Oncogenic mutant forms of MLL retain an ability to interact with menin but not other identified complex components. These studies link the menin tumor suppressor protein with the MLL histone methyltransferase machinery, with implications for Hox gene expression in development and leukemia pathogenesis.

Indexed as

Gene Expression RegulationProto-OncogenesCell Line, TumorDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHomeodomain ProteinsHost Cell Factor C1HumansK562 CellsLeukemiaMacromolecular SubstancesMyeloid-Lymphoid Leukemia ProteinProtein BindingProtein MethyltransferasesProteinsDNA-Binding ProteinsHCFC1 protein, humanHCFC2 protein, humanHistone-Lysine N-MethyltransferaseHistone Methyltransferaseshomeobox protein HOXA9Homeodomain ProteinsHost Cell Factor C1KMT2A protein, humanMacromolecular SubstancesMAS1 protein, humanMEN1 protein, humanMyeloid-Lymphoid Leukemia ProteinProtein MethyltransferasesProteinsProto-Oncogene MasProto-Oncogene ProteinsSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID15199122
PMCPMC480881
OpenAlexW2150056778

What OpenQuestion holds

Textmetadata
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.