ArticleNature communications2016
Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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.
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Who cites it
52 citing papers in PubMed, 74 citations in OpenAlex.
- Sam68 Exacerbates Pathologic Cardiac Hypertrophy by Suppressing Cardiomyocyte Glucose Oxidation.Circulation · 2026Article
- SAM68 is a multifunctional post-transcriptional regulator of cardiomyocyte differentiation.Nucleic acids research · 2026Article
- Host microRNA-31-5p regulates KHDRBS3 expression and modulates viral gene expression during KSHV lytic reactivation.Cell reports · 2026Article
- Held out wings RNA binding activity in the cytoplasm during early spermatogenesis.Communications biology · 2026Article
- Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins.Npj biosensing · 2026Article
- Roles of KHDRBS2 and KHDRBS3 in prostate cancer progression and AR-V7 regulation.Discover oncology · 2025Article
- Hypoxia-Induced circPRELID2 Promotes Gastric Cancer Metastasis by Facilitating ZEB2 Translation via PCBP1 O-GlcNAcylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Diverse roles of quaking in endothelial cell biology.Angiogenesis · 2025Review
- KH-R3H domain cooperation in RNA recognition by the global RNA-binding protein KhpB.Nature communications · 2025Article
- Chronic hypoxia induces alternative splicing of transcripts in the goldfish brain.Fish physiology and biochemistry · 2025Article
- RNA sculpting by the primordial Helix-clasp-Helix-Strand-Loop (HcH-SL) motif enforces chemical recognition enabling diverse KH domain functions.The Journal of biological chemistry · 2025Review
- Detection of hidden intronic DDC variant in aromatic L-amino acid decarboxylase deficiency by adaptive sampling.Journal of human genetics · 2024Article
- Role of Sam68 as an adaptor protein in inflammatory signaling.Cellular and molecular life sciences : CMLS · 2024Review
- 2'-Frontiers in molecular biosciences · 2024Article
- Multiple roles for AU-rich RNA binding proteins in the development of haematologic malignancies and their resistance to chemotherapy.RNA biology · 2024Review
- Development of Bifunctional, Raman Active Diyne-Girder Stapled α-Helical Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- The Role of Splicing Factors in Adipogenesis and Thermogenesis.Molecules and cells · 2023Review
- Structure and function analysis of Sam68 and hnRNP A1 synergy in the exclusion of exon 7 from SMN2 transcripts.Protein science : a publication of the Protein Society · 2023Article
- Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions.Nucleic acids research · 2022Article
- RNA-binding proteins of KHDRBS and IGF2BP families control the oncogenic activity of MLL-AF4.Nature communications · 2022Article
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 2 countries.
Funding
Abstract
Sam68 and T-STAR are members of the STAR family of proteins that directly link signal transduction with post-transcriptional gene regulation. Sam68 controls the alternative splicing of many oncogenic proteins. T-STAR is a tissue-specific paralogue that regulates the alternative splicing of neuronal pre-mRNAs. STAR proteins differ from most splicing factors, in that they contain a single RNA-binding domain. Their specificity of RNA recognition is thought to arise from their property to homodimerize, but how dimerization influences their function remains unknown. Here, we establish at atomic resolution how T-STAR and Sam68 bind to RNA, revealing an unexpected mode of dimerization different from other members of the STAR family. We further demonstrate that this unique dimerization interface is crucial for their biological activity in splicing regulation, and suggest that the increased RNA affinity through dimer formation is a crucial parameter enabling these proteins to select their functional targets within the transcriptome.
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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.