Evidence map›Paper›PMID 41581869›Full record

ArticleThe Journal of biological chemistry2026

A tryptophan-phenylalanine binding motif for the histone methyltransferases MLL4 and MLL3.

Soumi Biswas, Zohreh Tavaf, Caroline Benz, Moustafa Khalil, Dustin C Becht, Leandro Simonetti, M Andres Blanco, El Bachir Affar, Ylva Ivarsson, Tatiana G Kutateladze

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Soumi BiswasDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA.
Zohreh TavafDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA.
Caroline BenzDepartment of Chemistry for Life Sciences, Uppsala University, Uppsala, Sweden.
Moustafa KhalilCell Signaling and Cancer Research Unit, Maisonneuve-Rosemont Hospital Research Center, CIUSSS de l'Est-de-l'Ȋle de Montréal, Montréal, Quebec, Canada.
Dustin C BechtDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA.
Leandro SimonettiDepartment of Chemistry for Life Sciences, Uppsala University, Uppsala, Sweden.
M Andres BlancoDepartment of Biomedical Sciences, University of Pennsylvania, School of Veterinary Medicine, Philadelphia, Pennsylvania, USA.
El Bachir AffarCell Signaling and Cancer Research Unit, Maisonneuve-Rosemont Hospital Research Center, CIUSSS de l'Est-de-l'Ȋle de Montréal, Montréal, Quebec, Canada; Department of Medicine, University of Montréal, Montréal, Quebec, Canada.
Ylva IvarssonDepartment of Chemistry for Life Sciences, Uppsala University, Uppsala, Sweden.
Tatiana G KutateladzeDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA. Electronic address: tatiana.kutateladze@cuanschutz.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human methyltransferases mixed lineage leukemia 4 and 3 (MLL4 and MLL3) play pivotal roles in the regulation of epigenetic and transcriptional programs. Here, we report the identification and characterization of a tryptophan-phenylalanine binding motif recognized by MLL4 and MLL3. Binding of the sixth PHD finger of MLL4 and the seventh PHD finger of MLL3 to the tryptophan-phenylalanine motif derived from a set of human proteins was detected in a proteomic peptide-phage screening of intrinsically disordered regions of the human proteome and confirmed in NMR and MST assays. Mutational, genetic and binding interface analyses reveal the molecular mechanism underlying the direct interaction of MLL4 and MLL3 with the motif. A high correlation of expression of MLL4/MLL3 and the motif containing proteins in several tumor types suggests shared roles in oncogenic transcriptional programs. In conclusion, our findings highlight a potential relationship between the MLL4/MLL3 methyltransferases and diverse motif-containing epigenetic coregulators.

Indexed as

DNA-Binding ProteinsHistone-Lysine N-MethyltransferasePhenylalanineTryptophanAmino Acid MotifsBinding SitesHumansNuclear ProteinsProtein BindingDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseMLL4 protein, humanMLLT3 protein, humanNuclear ProteinsPhenylalanineTryptophaninteractionKMT2MLL3MLL4motifPHD finger

Identifiers

PMID41581869
PMCPMC12934300

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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.