ArticleScience (New York, N.Y.)2016
Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation.
Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 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
85 citing papers in PubMed.
- Article
- PINCH proteins orchestrate vascular mural cell homeostasis through integrated signaling and transcriptional networks.Angiogenesis · 2026Article
- Fine-tuning ERK activity enables proliferation-differentiation balance during lineage specification of human embryonic stem cells.PLoS biology · 2026Article
- ELK1 promotes the progress of myeloid leukemia by hindering the differentiation of neutrophils.Experimental hematology & oncology · 2026Article
- Advances in Tumor-Derived Exosomal Non-Coding RNAs Regulating M2 Macrophage Polarization: Molecular Mechanisms and Signaling Pathway.Cancer medicine · 2025Review
- MPK6-mediated phosphorylation destabilizes MYC2 and attenuates its transcriptional activity in jasmonate signaling.Plant communications · 2025Article
- Decoding protein N-phosphorylation functionality and sequence patterns.Briefings in bioinformatics · 2025Article
- Sequence- and Docking-Site-Dependent Contributions to Multi-Site Phosphorylation of an Intrinsically Disordered MAPK Substrate.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structural basis of human Mediator recruitment by the phosphorylated transcription factor Elk-1.Nature communications · 2025Article
- Functional profiling of serine, threonine and tyrosine sites.Nature chemical biology · 2025Article
- Virally mediated expression of a biologically active peptide to restrain the nuclear functions of ERK1/2 attenuates learning extinction but not acquisition.Molecular brain · 2025Article
- Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The CDK9-SPT5 Axis in Control of Transcription Elongation by RNAPII.Journal of molecular biology · 2025Review
- NEMO-Binding Domain/IKKγ Inhibitory Peptide Alleviates Neuronal Pyroptosis in Spinal Cord Injury by Inhibiting ASMase-Induced Lysosome Membrane Permeabilization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Regulation of developmentally controlled enhancer activity by extrinsic signals in normal and malignant cells: AP-1 at the centre.Frontiers in epigenetics and epigenomics · 2024Article
- Cyclic Ion Mobility-Mass Spectrometry and Tandem Collision Induced Unfolding for Quantification of Elusive Protein Biomarkers.Analytical chemistry · 2024Article
- Small-molecule α-lipoic acid targets ELK1 to balance human neutrophil and erythrocyte differentiation.Stem cell research & therapy · 2024Article
- Review
- N-terminal alanine-rich (NTAR) sequences drive precise start codon selection resulting in elevated translation of multiple proteins including ERK1/2.Nucleic acids research · 2023Article
- Intrinsically disordered proteins and conformational noise: The hypothesis a decade later.iScience · 2023Review
25 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors.
Funding
Abstract
Multisite phosphorylation regulates many transcription factors, including the serum response factor partner Elk-1. Phosphorylation of the transcriptional activation domain (TAD) of Elk-1 by the protein kinase ERK at multiple sites potentiates recruitment of the Mediator transcriptional coactivator complex and transcriptional activation, but the roles of individual phosphorylation events had remained unclear. Using time-resolved nuclear magnetic resonance spectroscopy, we found that ERK2 phosphorylation proceeds at markedly different rates at eight TAD sites in vitro, which we classified as fast, intermediate, and slow. Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output. Progressive Elk-1 phosphorylation thus ensures a self-limiting response to ERK activation, which occurs independently of antagonizing phosphatase activity.
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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.