ArticleNature structural & molecular biology2009
Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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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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
58 citing papers in PubMed, 100 citations in OpenAlex.
- Cysteine thiol-to-sulfonate oxidation induces unfolding for the functional switching of the extracellular HMGB1 protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The RNA-Binding Protein KSRP Is a Negative Regulator of Innate Immunity.Biomolecules · 2025Review
- Balancing LncRNA H19 and miR-675 Bioconversion as a Key Regulator of Embryonic Myogenesis Under Maternal Obesity.Journal of cachexia, sarcopenia and muscle · 2025Article
- Expanding the Functions of KHSRP Protein: Insights into DNA G-Quadruplex Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The therapeutic potential of RNA m(6)A in lung cancer.Cell communication and signaling : CCS · 2024Review
- Phosphorylation by Protein Kinase C Weakens DNA-Binding Affinity and Folding Stability of the HMGB1 Protein.Biochemistry · 2024Article
- Increased ANKRD1 Levels in Early Senescence Mediated by RBMS1-ElicitedMolecular and cellular biology · 2024Article
- KHSRP knockdown inhibits papillary renal cell carcinoma progression and sensitizes to gemcitabine.Frontiers in pharmacology · 2024Article
- K-Homology Type Splicing Regulatory Protein: Mechanism of Action in Cancer and Immune Disorders.Critical reviews in eukaryotic gene expression · 2024Article
- The Role of KH-Type Splicing Regulatory Protein (KSRP) for Immune Functions and Tumorigenesis.Cells · 2022Review
- Molecular Mechanisms of Parathyroid Disorders in Chronic Kidney Disease.Metabolites · 2022Review
- AlphaFold 2 and NMR Spectroscopy: Partners to Understand Protein Structure, Dynamics and Function.Frontiers in molecular biosciences · 2022Review
- Article
- De novo design of tyrosine and serine kinase-driven protein switches.Nature structural & molecular biology · 2021Article
- Post-translational Control of RNA-Binding Proteins and Disease-Related Dysregulation.Frontiers in molecular biosciences · 2021Review
- Article
- Exploring protein phosphorylation by combining computational approaches and biochemical methods.Computational and structural biotechnology journal · 2020Article
- RNA-binding protein KHSRP promotes tumor growth and metastasis in non-small cell lung cancer.Journal of experimental & clinical cancer research : CR · 2019Article
- Emerging Evidence of Translational Control by AU-Rich Element-Binding Proteins.Frontiers in genetics · 2019Review
- Enzymatic Control of the Conformational Landscape of Self-Assembling Peptides.Angewandte Chemie (International ed. in English) · 2018Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
Abstract
The AU-rich element (ARE)-mediated mRNA-degradation activity of the RNA binding K-homology splicing regulator protein (KSRP) is regulated by phosphorylation of a serine within its N-terminal KH domain (KH1). In the cell, phosphorylation promotes the interaction of KSRP and 14-3-3zeta protein and impairs the ability of KSRP to promote the degradation of its RNA targets. Here we examine the molecular details of this mechanism. We report that phosphorylation leads to the unfolding of the structurally atypical and unstable KH1, creating a site for 14-3-3zeta binding. Using this site, 14-3-3zeta discriminates between phosphorylated and unphosphorylated KH1, driving the nuclear localization of KSRP. 14-3-3zeta -KH1 interaction regulates the mRNA-decay activity of KSRP by sequestering the protein in a separate functional pool. This study demonstrates how an mRNA-degradation pathway is connected to extracellular signaling networks through the reversible unfolding of a protein domain.
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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.