ArticleMolecular and cellular biology2013
Quantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.
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Who cites it
150 citing papers in PubMed.
- Promiscuous RNA binding by WDR5 remodels the KMT2A (MLL1) histone methyltransferase complex to an inactive state.Molecular cell · 2026Article
- Role of PER-WDR5 interactions in the mammalian circadian clock.Nature communications · 2026Article
- RYBP regulates selective genomic binding of TrxG and PcG components in embryonic stem cell fate control.The EMBO journal · 2026Article
- Promiscuous RNA binding by WDR5 remodels the KMT2A (MLL1) histone methyltransferase complex to an inactive state.bioRxiv : the preprint server for biology · 2026Article
- Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026Review
- A busy BOD1-y: the diverse functions of an intracellular signaling regulatory protein family.Biochemical Society transactions · 2025Review
- KMT2A-rearranged leukemia: from mechanism to drug development.Experimental hematology · 2025Review
- Article
- Modelling transcription with explainable AI uncovers context-specific epigenetic gene regulation at promoters and gene bodies.PLoS genetics · 2025Article
- Combined inhibition of KAT6A/B and Menin reverses estrogen receptor-driven gene expression programs in breast cancer.Cell reports. Medicine · 2025Article
- MLL/WDR5 complex recruits centriolar satellite protein Cep72 to regulate microtubule nucleation and spindle formation.Science advances · 2024Article
- Polycomb protein RYBP facilitates super-enhancer activity.Molecular medicine (Cambridge, Mass.) · 2024Article
- O-GlcNAc transferase congenital disorder of glycosylation (OGT-CDG): Potential mechanistic targets revealed by evaluating the OGT interactome.The Journal of biological chemistry · 2024Review
- Reduction of ZFX levels decreases histone H4 acetylation and increases Pol2 pausing at target promoters.Nucleic acids research · 2024Article
- Unveiling the Molecular Landscape of Pancreatic Ductal Adenocarcinoma: Insights into the Role of the COMPASS-like Complex.International journal of molecular sciences · 2024Review
- KMT2 Family of H3K4 Methyltransferases: Enzymatic Activity-dependent and -independent Functions.Journal of molecular biology · 2024Review
- KMT2D preferentially binds mRNAs of the genes it regulates, suggesting a role in RNA processing.Protein science : a publication of the Protein Society · 2024Article
- Restrictor synergizes with Symplekin and PNUTS to terminate extragenic transcription.Genes & development · 2023Article
- The pseudokinase TRIB3 controls adipocyte lipid homeostasis and proliferation in vitro and in vivo.Molecular metabolism · 2023Article
- In Vivo and In Vitro Characterization of the RNA Binding Capacity of SETD1A (KMT2F).International journal of molecular sciences · 2023Article
90 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
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Abstract
Methylation of lysine 4 on histone H3 (H3K4) at promoters is tightly linked to transcriptional regulation in human cells. At least six different COMPASS-like multisubunit (SET1/MLL) complexes that contain methyltransferase activity for H3K4 have been described, but a comprehensive and quantitative analysis of these SET1/MLL complexes is lacking. We applied label-free quantitative mass spectrometry to determine the subunit composition and stoichiometry of the human SET1/MLL complexes. We identified both known and novel, unique and shared interactors and determined their distribution and stoichiometry over the different SET1/MLL complexes. In addition to being a core COMPASS subunit, the Dpy30 protein is a genuine subunit of the NURF chromatin remodeling complex. Furthermore, we identified the Bod1 protein as a discriminator between the SET1B and SET1A complexes, and we show that the H3K36me-interactor Psip1 preferentially binds to the MLL2 complex. Finally, absolute protein quantification in crude lysates mirrors many of the observed SET1/MLL complex stoichiometries. Our findings provide a molecular framework for understanding the diversity and abundance of the different SET1/MLL complexes, which together establish the H3K4 methylation landscape in human cells.
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