ArticleNucleic acids research2008
The sequence selectivity of KSRP explains its flexibility in the recognition of the RNA targets.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 66 citations in OpenAlex.
- A novel small molecule inhibitor targeting KHSRP methylation suppresses colon cancer progression.Acta pharmaceutica Sinica. B · 2026Article
- A novel NLP-based method and algorithm to discover RNA-binding protein (RBP) motifs, contexts, binding preferences, and interactions.RNA (New York, N.Y.) · 2026Article
- RNA-Binding Proteins: Modulators of Canonical Wnt Signaling Pathway.International journal of molecular sciences · 2025Review
- K-Homology Splicing Regulatory Protein (KSRP) Augments Survival and Proliferation of Human Melanoma Cells.Current issues in molecular biology · 2025Article
- Expanding the Functions of KHSRP Protein: Insights into DNA G-Quadruplex Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes.Journal of structural biology: X · 2024Article
- DeepLocRNA: an interpretable deep learning model for predicting RNA subcellular localization with domain-specific transfer-learning.Bioinformatics (Oxford, England) · 2024Article
- K-Homology Type Splicing Regulatory Protein: Mechanism of Action in Cancer and Immune Disorders.Critical reviews in eukaryotic gene expression · 2024Article
- Identification of proteins that bind extracellular microRNAs secreted by the parasitic nematode Trichinella spiralis.Biology open · 2023Article
- Cooperativity boosts affinity and specificity of proteins with multiple RNA-binding domains.NAR genomics and bioinformatics · 2023Article
- Two distinct binding modes provide the RNA-binding protein RbFox with extraordinary sequence specificity.Nature communications · 2023Article
- TGF-β1 modulates temozolomide resistance in glioblastoma via altered microRNA processing and elevated MGMT.Neuro-oncology · 2021Article
- FMRP - G-quadruplex mRNA - miR-125a interactions: Implications for miR-125a mediated translation regulation of PSD-95 mRNA.PloS one · 2019Article
- A method for the unbiased and efficient segmental labelling of RNA-binding proteins for structure and biophysics.Scientific reports · 2017Article
- Both Maintenance and Avoidance of RNA-Binding Protein Interactions Constrain Coding Sequence Evolution.Molecular biology and evolution · 2017Article
- RNA Binding Protein Regulation and Cross-Talk in the Control of AU-rich mRNA Fate.Frontiers in molecular biosciences · 2017Review
- A novel p70 S6 kinase-microRNA biogenesis axis mediates multicellular spheroid formation in ovarian cancer progression.Oncotarget · 2016Article
- Protein-RNA specificity by high-throughput principal component analysis of NMR spectra.Nucleic acids research · 2015Article
- HnRNP A1 tethers KSRP to an exon splicing silencer that inhibits an erythroid-specific splicing event in PU.1-induced erythroleukemia.American journal of cancer research · 2015Article
- A central role for the primary microRNA stem in guiding the position and efficiency of Drosha processing of a viral pri-miRNA.RNA (New York, N.Y.) · 2014Article
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4 authors.
Funding
Abstract
K-homology (KH) splicing regulator protein (KSRP) is a multi-domain RNA-binding protein that regulates different steps of mRNA metabolism, from mRNA splicing to mRNA decay, interacting with a broad range of RNA sequences. To understand how KSRP recognizes its different RNA targets it is necessary to define the general rules of KSRP-RNA interaction. We describe here a complete scaffold-independent analysis of the RNA-binding potential of the four KH domains of KSRP. The analysis shows that KH3 binds to the RNA with a significantly higher affinity than the other domains and recognizes specifically a G-rich target. It also demonstrates that the other KH domains of KSRP display different sequence preferences explaining the broad range of targets recognized by the protein. Further, KSRP shows a strong negative selectivity for sequences containing several adjacent Cytosines limiting the target choice of KSRP within single-stranded RNA regions. The in-depth analysis of the RNA-binding potential of the KH domains of KSRP provides us with an understanding of the role of low sequence specificity domains in RNA recognition by multi-domain RNA-binding proteins.
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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.