ArticleJournal of cell science2005
Active ERK1 is dimerized in vivo: bisphosphodimers generate peak kinase activity and monophosphodimers maintain basal ERK1 activity.
Article in Journal of cell science, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- GCN5-ERK lactylation-phosphorylation loop amplifies lactate-driven cancer progression.Nature chemical biology · 2026Article
- Regulatory differences between atypical and typical MAP kinases in Dictyostelium discoideum.Cellular signalling · 2025Article
- ERK1/2 mitogen-activated protein kinase dimerization is essential for the regulation of cell motility.Molecular oncology · 2025Article
- TLR7 Agonists Modulate the Activation of Human Conjunctival Epithelial Cells Induced by IL-1β via the ERK1/2 Signaling Pathway.Inflammation · 2023Article
- Review
- The MEK/ERK Network as a Therapeutic Target in Human Cancer.Molecular cancer research : MCR · 2021Review
- Aspergillus fumigatus Hsp90 interacts with the main components of the cell wall integrity pathway and cooperates in heat shock and cell wall stress adaptation.Cellular microbiology · 2021Article
- Beyond Kinase Activity: ERK5 Nucleo-Cytoplasmic Shuttling as a Novel Target for Anticancer Therapy.International journal of molecular sciences · 2020Review
- Monomeric and dimeric models of ERK2 in conjunction with studies on cellular localization, nuclear translocation, and in vitro analysis.Molecules and cells · 2012Review
- Activated ERK2 is a monomer in vitro with or without divalent cations and when complexed to the cytoplasmic scaffold PEA-15.Biochemistry · 2011Article
- Homodimerization of Nemo-like kinase is essential for activation and nuclear localization.Molecular biology of the cell · 2011Article
- Aconitase regulation of erythropoiesis correlates with a novel licensing function in erythropoietin-induced ERK signaling.PloS one · 2011Article
- ERK nuclear translocation is dimerization-independent but controlled by the rate of phosphorylation.The Journal of biological chemistry · 2010Article
- Noncatalytic function of ERK1/2 can promote Raf/MEK/ERK-mediated growth arrest signaling.The Journal of biological chemistry · 2009Article
- A new paradigm for MAPK: structural interactions of hERK1 with mitochondria in HeLa cells.PloS one · 2009Article
- MAP kinase dependent cyclinE/cdk2 activity promotes DNA replication in early sea urchin embryos.Developmental biology · 2009Article
- Sensitivity analysis predicts that the ERK-pMEK interaction regulates ERK nuclear translocation.IET systems biology · 2009Article
- Protein scaffolds in MAP kinase signalling.Cellular signalling · 2009Review
- Mitochondrially localized ERK2 regulates mitophagy and autophagic cell stress: implications for Parkinson's disease.Autophagy · 2008Article
- Calcium signalling in early embryos.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2008Review
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
ERK1 and ERK2 are widely involved in cell signalling. Using a recombinant approach, it has been shown that exogenous ERK2 is capable of dimerization and that preventing dimerization reduces its nuclear accumulation on stimulation. Dimerization occurs on phosphorylation; the dimer partner of phosphorylated ERK2 may be either phosphorylated or unphosphorylated. It has been assumed that monophosphodimers are hemiactive. Here we show that ERK1 is capable of dimerization both in vivo and in vitro. Dimerization of human recombinant ERK1 in vitro requires both ERK1 phosphorylation and cellular cofactor(s); it leads to the formation of a high molecular weight complex that can be dissociated by treatment with beta-mercaptoethanol. We demonstrate for the first time in both sea urchin embryos and human cells that native ERK forms dimers and that high ERK kinase activity is largely associated with bisphosphodimers, not with monophosphodimers or phosphorylated monomers. The activity of the bisphosphodimer is about 20-fold higher than that of the phosphorylated monomer in vitro and the bisphosphodimer shows 5- to 7-fold higher in vivo activity than the basal activity attributable to the monophosphodimer. Thus phosphorylation of both partners in the dimer is a hallmark of ERK activation. Judgments made about ERK kinase activity associated with phosphorylated monomers are at best a proxy for ERK activity.
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What OpenQuestion holds
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.