ArticleNature communications2023
The SPOC domain is a phosphoserine binding module that bridges transcription machinery with co- and post-transcriptional regulators.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 32 citations in OpenAlex.
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- Why does the m6A writer complex require so many proteins?PLoS biology · 2025Review
- RBM15-MKL1 fusion protein promotes leukemia via m6A methylation and Wnt pathway activation.Blood · 2025Article
- Role of N6-methyladenosine methyltransferase component RBM15 in cancer progression and its therapeutic potential.Discover oncology · 2025Review
- The chromatin reader Dido3 is a regulator of the gene network that controls B cell differentiation.Cell & bioscience · 2025Article
- LEDGF/p75 promotes transcriptional pausing through preventing SPT5 phosphorylation.Science advances · 2025Article
- Structure and Methyl-lysine Binding Selectivity of the HUSH Complex Subunit MPP8.Journal of molecular biology · 2025Article
- RBM15-mediated metabolic reprogramming boosts immune response in colorectal cancer.Frontiers in immunology · 2025Article
- Hypoxia-Induced Histone Lactylation Drives Cisplatin Resistance in Bladder Cancer by Promoting RBM15-Dependent mResearch (Washington, D.C.) · 2025Article
- Structures and mechanisms of the RNA mActa biochimica et biophysica Sinica · 2024Review
- Identification of RBM15 as a prognostic biomarker in prostate cancer involving the regulation of prognostic m6A-related lncRNAs.European journal of medical research · 2024Article
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- The mExperimental & molecular medicine · 2024Article
- C19ORF84 connects piRNA and DNA methylation machineries to defend the mammalian germ line.Molecular cell · 2024Article
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- Exploring the role of mFrontiers in oncology · 2024Review
Corrections and comments
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Authors and funding
16 authors at 4 institutions in 4 countries.
Funding
Abstract
The heptad repeats of the C-terminal domain (CTD) of RNA polymerase II (Pol II) are extensively modified throughout the transcription cycle. The CTD coordinates RNA synthesis and processing by recruiting transcription regulators as well as RNA capping, splicing and 3'end processing factors. The SPOC domain of PHF3 was recently identified as a CTD reader domain specifically binding to phosphorylated serine-2 residues in adjacent CTD repeats. Here, we establish the SPOC domains of the human proteins DIDO, SHARP (also known as SPEN) and RBM15 as phosphoserine binding modules that can act as CTD readers but also recognize other phosphorylated binding partners. We report the crystal structure of SHARP SPOC in complex with CTD and identify the molecular determinants for its specific binding to phosphorylated serine-5. PHF3 and DIDO SPOC domains preferentially interact with the Pol II elongation complex, while RBM15 and SHARP SPOC domains engage with writers and readers of m
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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 Socratic graph.