ArticleNature communications2021
Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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.
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.
Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Discovery of High-Affinity Peptide Ligands Targeting the SPIN1 Tudor 3 Domain Via a Minimalist Pruning Strategy.ACS medicinal chemistry letters · 2026Article
- Single-cell transcriptomics and functional analyses identified SPIN.DOC as a regulator for Wnt signaling and cancer stemness in colorectal cancer.Human cell · 2026Article
- Overexpressed Spindlin1 relocalizes to the nucleoli during fixation.Biochemistry and biophysics reports · 2026Article
- HBV HBx protein masks epigenetic reader Spindlin1 via an inter-molecular zinc finger to subvert transcriptional control.Nature communications · 2026Article
- Development of Dimethylsulfonium Probes for Broad Profiling of Methyllysine Reader Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Evaluation of Cooperative Binding of Histone Post-Translational Modifications and the Surrounding Sequence by Trimethyllysine Reader Proteins.Biochemistry · 2025Article
- Role of Histone H3 Lysine 4 Methylation in Chromatin Biology.Molecules (Basel, Switzerland) · 2025Review
- Review
- The subcortical maternal complex safeguards mouse oocyte-to-embryo transition by preventing nuclear entry of SPIN1.Nature structural & molecular biology · 2025Article
- Immune-modulatory effects of Spindlin-1 inhibitors.Clinical and experimental immunology · 2025Article
- SPIN.DOC induces cellular transformation of NIH3T3 normal mouse fibroblast cells.Molecular biology research communications · 2025Article
- Phase separation of SPIN1 through its IDR facilitates histone methylation readout and tumorigenesis.Journal of molecular cell biology · 2024Article
- Article
- SPIN1 facilitates chemoresistance and HR repair by promoting Tip60 binding to H3K9me3.EMBO reports · 2024Article
- Discovery of a Potent, Selective, and Cell-Active SPIN1 Inhibitor.Journal of medicinal chemistry · 2024Article
- Molecular insights into Spindlin1-HBx interplay and its impact on HBV transcription from cccDNA minichromosome.Nature communications · 2023Article
- Real-time imaging of RNA polymerase I activity in living human cells.The Journal of cell biology · 2023Article
- Cocaine regulation of Nr4a1 chromatin bivalency and mRNA in male and female mice.Scientific reports · 2022Article
- Catching Nucleosome by Its Decorated Tails Determines Its Functional States.Frontiers in genetics · 2022Review
- SPINDOC binds PARP1 to facilitate PARylation.Nature communications · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spindlin1 is a unique multivalent epigenetic reader that facilitates ribosomal RNA transcription. In this study, we provide molecular and structural basis by which Spindlin1 acts in complex with C11orf84 to preferentially recognize non-canonical bivalent mark of trimethylated lysine 4 and lysine 9 present on the same histone H3 tail (H3K4me3K9me3). We demonstrate that C11orf84 binding stabilizes Spindlin1 and enhances its association with bivalent H3K4me3K9me3 mark. The functional analysis suggests that Spindlin1/C11orf84 complex can displace HP1 proteins from H3K4me3K9me3-enriched rDNA loci, thereby facilitating the conversion of these poised rDNA repeats from the repressed state to the active conformation, and the consequent recruitment of RNA Polymerase I for rRNA transcription. Our study uncovers a previously unappreciated mechanism of bivalent H3K4me3K9me3 recognition by Spindlin1/C11orf84 complex required for activation of rRNA transcription.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.