ArticleNature communications2017
Heme enables proper positioning of Drosha and DGCR8 on primary microRNAs.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 41 papers.
What it found
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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.
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Who cites it
41 citing papers in PubMed, 66 citations in OpenAlex.
- DGCR8 regulates multiple processes of transcription coupled nucleotide excision repair.Scientific reports · 2026Article
- An intrinsically disordered region of Drosha selectively promotes miRNA biogenesis independent of tissue-specific Microprocessor condensates.Genes & development · 2026Article
- The Life of MicroRNAs: Biogenesis, Function and Decay in Cancer.Biomolecules · 2025Review
- Non-Canonical Compartmentalization of DROSHA Protein at the Golgi Apparatus: miRNA Biogenesis-Independent Functionality in Human Cancer Cells of Diverse Tissue Origin.International journal of molecular sciences · 2025Article
- HOTTIP suppresses ferroptosis via mediating DGCR8/miR‑214‑3p/GPX4 regulatory axis in osteosarcoma.Oncology reports · 2025Article
- Assessing Microprocessor complex mutations with a Microsensor system.RNA (New York, N.Y.) · 2025Article
- The biogenesis and regulation of animal microRNAs.Nature reviews. Molecular cell biology · 2025Review
- The structural landscape of Microprocessor-mediated processing of pri-let-7 miRNAs.Molecular cell · 2024Article
- The structural landscape of Microprocessor mediated pri-bioRxiv : the preprint server for biology · 2024Article
- Parallel degradome-seq and DMS-MaPseq substantially revise the miRNA biogenesis atlas in Arabidopsis.Nature plants · 2024Article
- Regulating Protein-RNA Interactions: Advances in Targeting the LIN28/Let-7 Pathway.International journal of molecular sciences · 2024Review
- Gas-sensing riboceptors.RNA biology · 2024Article
- microRNAs in action: biogenesis, function and regulation.Nature reviews. Genetics · 2023Review
- Redox-Mediated Rewiring of Signalling Pathways: The Role of a Cellular Clock in Brain Health and Disease.Antioxidants (Basel, Switzerland) · 2023Review
- N6-methyladenosine (m6A) methyltransferase WTAP-mediated miR-92b-5p accelerates osteoarthritis progression.Cell communication and signaling : CCS · 2023Article
- Role of the proline-rich disordered domain of DROSHA in intronic microRNA processing.Genes & development · 2023Article
- SRSF7 and SRSF3 depend on RNA sequencing motifs and secondary structures to regulate Microprocessor.Life science alliance · 2023Article
- Depletion assisted hemin affinity (DAsHA) proteomics reveals an expanded landscape of heme-binding proteins in the human proteome.Metallomics : integrated biometal science · 2023Article
- Dynamic Protein-RNA recognition in primary MicroRNA processing.Current opinion in structural biology · 2022Review
- Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022Review
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
MicroRNAs regulate the expression of many proteins and require specific maturation steps. Primary microRNA transcripts (pri-miRs) are cleaved by Microprocessor, a complex containing the RNase Drosha and its partner protein, DGCR8. Although DGCR8 is known to bind heme, the molecular role of heme in pri-miR processing is unknown. Here we show that heme is critical for Microprocessor to process pri-miRs with high fidelity. Furthermore, the degree of inherent heme dependence varies for different pri-miRs. Heme-dependent pri-miRs fail to properly recruit Drosha, but heme-bound DGCR8 can correct erroneous binding events. Rather than changing the oligomerization state, heme induces a conformational change in DGCR8. Finally, we demonstrate that heme activates DGCR8 to recognize pri-miRs by specifically binding the terminal loop near the 3' single-stranded segment.
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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.