ArticleThe Journal of biological chemistry2001
A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission.
Article in The Journal of biological chemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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Who cites it
82 citing papers in PubMed, 180 citations in OpenAlex.
- ERK pathway reactivation prevents anthrax toxin lethality in mice.Nature microbiology · 2025Article
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- Linear motif specificity in signaling through p38α and ERK2 mitogen-activated protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The WW domain of IQGAP1 binds directly to the p110α catalytic subunit of PI 3-kinase.The Biochemical journal · 2023Article
- ERK2 MAP kinase regulates SUFU binding by multisite phosphorylation of GLI1.Life science alliance · 2022Article
- TOR complex 2 is a master regulator of plasma membrane homeostasis.The Biochemical journal · 2022Article
- Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.The Biochemical journal · 2022Review
- Genomic profiling and network-level understanding uncover the potential genes and the pathways in hepatocellular carcinoma.Frontiers in genetics · 2022Article
- The ERK mitogen-activated protein kinase signaling network: the final frontier in RAS signal transduction.Biochemical Society transactions · 2021Review
- How to Annotate and Submit a Short Linear Motif to the Eukaryotic Linear Motif Resource.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Targeting ERK beyond the boundaries of the kinase active site in melanoma.Molecular carcinogenesis · 2019Review
- Miles to go (mtgo) encodes FNDC3 proteins that interact with the chaperonin subunit CCT3 and are required for NMJ branching and growth in Drosophila.Developmental biology · 2019Article
- Allosteric Modulation of JNK Docking Site Interactions with ATP-Competitive Inhibitors.Biochemistry · 2018Article
- Comparative analysis of plant MKK gene family reveals novel expansion mechanism of the members and sheds new light on functional conservation.BMC genomics · 2018Article
- Analysis of the thresholds for transcriptional activation by the yeast MAP kinases Fus3 and Kss1.Molecular biology of the cell · 2018Article
- Endogenous, regulatory cysteine sulfenylation of ERK kinases in response to proliferative signals.Free radical biology & medicine · 2017Article
- The WW domain of the scaffolding protein IQGAP1 is neither necessary nor sufficient for binding to the MAPKs ERK1 and ERK2.The Journal of biological chemistry · 2017Article
- Optical control of cell signaling by single-chain photoswitchable kinases.Science (New York, N.Y.) · 2017Article
- Shift of microRNA profile upon orthotopic xenografting of glioblastoma spheroid cultures.Journal of neuro-oncology · 2016Article
22 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The recognition of mitogen-activated protein kinases (MAPKs) by their upstream activators, MAPK/ERK kinases (MEKs), is crucial for the effective and accurate transmission of many signals. We demonstrated previously that the yeast MAPKs Kss1 and Fus3 bind with high affinity to the N terminus of the MEK Ste7, and proposed that a conserved motif in Ste7, the MAPK-docking site, mediates this interaction. Here we show that the corresponding sequences in human MEK1 and MEK2 are necessary and sufficient for the direct binding of the MAPKs ERK1 and ERK2. Mutations in MEK1, MEK2, or Ste7 that altered conserved residues in the docking site diminished binding of the cognate MAPKs. Furthermore, short peptides corresponding to the docking sites in these MEKs inhibited MEK1-mediated phosphorylation of ERK2 in vitro. In yeast cells, docking-defective alleles of Ste7 were modestly compromised in their ability to transmit the mating pheromone signal. This deficiency was dramatically enhanced when the ability of the Ste5 scaffold protein to associate with components of the MAPK cascade was also compromised. Thus, both the MEK-MAPK docking interaction and binding to the Ste5 scaffold make mutually reinforcing contributions to the efficiency of signaling by this MAPK cascade in vivo.
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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.