ArticleMolecular systems biology2013
Phosphoproteome dynamics reveal novel ERK1/2 MAP kinase substrates with broad spectrum of functions.
Article in Molecular systems biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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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
55 citing papers in PubMed, 155 citations in OpenAlex.
- Phosphoproteomics identifies the DYRK1B protein kinase as a regulator of processing bodies.Journal of cell science · 2026Article
- Profiling protein post-translational modifications in plasma-derived extracellular vesicles as fingerprints for breast cancer subtypes.Genome biology · 2026Article
- MAPK/ERK signaling regulates H3K9me3 heterochromatin reorganization to confer mesendoderm developmental competence.Nucleic acids research · 2026Article
- Localized heat induces ERK activation and signal propagation in solid tumors.Scientific reports · 2026Article
- Oncogenic KRAS/ERK/JUNB signaling suppresses differentiation regulator GATA6 in pancreatic cancer.The Journal of clinical investigation · 2026Article
- JUNB and JUND in Urological Cancers: A Literature Review.Current issues in molecular biology · 2025Review
- MAPK/ERK signaling blocks ectopic H3K9me3 heterochromatin formation to confer mesoderm and endoderm developmental competence.bioRxiv : the preprint server for biology · 2025Article
- StageTip: a little giant unveiling the potential of mass spectrometry-based proteomics.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025Review
- ZO-1 interacts with YB-1 in endothelial cells to regulate stress granule formation during angiogenesis.Nature communications · 2024Article
- Navigating the ERK1/2 MAPK Cascade.Biomolecules · 2023Review
- Protocadherin gamma C3: a new player in regulating vascular barrier function.Neural regeneration research · 2023Review
- Article
- A Comprehensive Outlook on Dilated Cardiomyopathy (DCM): State-Of-The-Art Developments with Special Emphasis on OMICS-Based Approaches.Journal of cardiovascular development and disease · 2022Review
- Harnessing RKIP to Combat Heart Disease and Cancer.Cancers · 2022Review
- Roles of peptidyl prolyl isomerase Pin1 in viral propagation.Frontiers in cell and developmental biology · 2022Review
- CG6015 controls spermatogonia transit-amplifying divisions by epidermal growth factor receptor signaling in Drosophila testes.Cell death & disease · 2021Article
- The ERK mitogen-activated protein kinase signaling network: the final frontier in RAS signal transduction.Biochemical Society transactions · 2021Review
- TGFβ promotes widespread enhancer chromatin opening and operates on genomic regulatory domains.Nature communications · 2020Article
- Article
- The inotropic agent digitoxin strengthens desmosomal adhesion in cardiac myocytes in an ERK1/2-dependent manner.Basic research in cardiology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The ERK1/2 MAP kinase pathway is an evolutionarily conserved signaling module that controls many fundamental physiological processes. Deregulated activity of ERK1/2 MAP kinases is associated with developmental syndromes and several human diseases. Despite the importance of this pathway, a comprehensive picture of the natural substrate repertoire and biochemical mechanisms regulated by ERK1/2 is still lacking. In this study, we used large-scale quantitative phosphoproteomics and bioinformatics analyses to identify novel candidate ERK1/2 substrates based on their phosphorylation signature and kinetic profiles in epithelial cells. We identified a total of 7936 phosphorylation sites within 1861 proteins, of which 155 classify as candidate ERK1/2 substrates, including 128 new targets. Candidate ERK1/2 substrates are involved in diverse cellular processes including transcriptional regulation, chromatin remodeling, RNA splicing, cytoskeleton dynamics, cellular junctions and cell signaling. Detailed characterization of one newly identified substrate, the transcriptional regulator JunB, revealed that ERK1/2 phosphorylate JunB on a serine adjacent to the DNA-binding domain, resulting in increased DNA-binding affinity and transcriptional activity. Our study expands the spectrum of cellular functions controlled by ERK1/2 kinases.
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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.