ArticleThe Journal of biological chemistry2013
Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- Multiple overlapping SNARE complexes drive endosome maturation in Drosophila nephrocytes.Nature communications · 2026Article
- Structural basis for MEKK2 dimerization and substrate recognition.Nature communications · 2025Article
- Combined Physics- and Machine-Learning-Based Method to Identify Druggable Binding Sites Using SILCS-Hotspots.Journal of chemical information and modeling · 2024Article
- Essential Oils from the Leaves, Stem, and Roots ofMolecules (Basel, Switzerland) · 2022Article
- Profiling MAP kinase cysteines for targeted covalent inhibitor design.RSC medicinal chemistry · 2022Article
- The MEK5/ERK5 Pathway in Health and Disease.International journal of molecular sciences · 2021Review
- Amino Acids in Cell Signaling: Regulation and Function.Advances in experimental medicine and biology · 2021Article
- Co-regulation of the transcription controlling ATF2 phosphoswitch by JNK and p38.Nature communications · 2020Article
- MAP Kinase-Mediated Activation of RSK1 and MK2 Substrate Kinases.Structure (London, England : 1993) · 2020Article
- Identification and characterization of fragment binding sites for allosteric ligand design using the site identification by ligand competitive saturation hotspots approach (SILCS-Hotspots).Biochimica et biophysica acta. General subjects · 2020Article
- Up-regulation of DcR3 in microbial toxins-stimulated HUVECs involves NF-κB signalling.BMC biochemistry · 2018Article
- Homing in: Mechanisms of Substrate Targeting by Protein Kinases.Trends in biochemical sciences · 2018Review
- Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion.PLoS genetics · 2018Article
- Rab2 promotes autophagic and endocytic lysosomal degradation.The Journal of cell biology · 2017Article
- Article
- The Kinome of Pacific Oyster Crassostrea gigas, Its Expression during Development and in Response to Environmental Factors.PloS one · 2016Article
- Systematic discovery of linear binding motifs targeting an ancient protein interaction surface on MAP kinases.Molecular systems biology · 2015Article
- Extracellular signal-regulated kinase 5 promotes acute cellular and systemic inflammation.Science signaling · 2015Article
- Structure and dynamics of the MKK7-JNK signaling complex.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Co-conserved MAPK features couple D-domain docking groove to distal allosteric sites via the C-terminal flanking tail.PloS one · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mitogen-activated protein kinase (MAPK) activation depends on a linear binding motif found in all MAPK kinases (MKK). In addition, the PB1 (Phox and Bem1) domain of MKK5 is required for extracellular signal regulated kinase 5 (ERK5) activation. We present the crystal structure of ERK5 in complex with an MKK5 construct comprised of the PB1 domain and the linear binding motif. We show that ERK5 has distinct protein-protein interaction surfaces compared with ERK2, which is the closest ERK5 paralog. The two MAPKs have characteristically different physiological functions and their distinct protein-protein interaction surface topography enables them to bind different sets of activators and substrates. Structural and biochemical characterization revealed that the MKK5 PB1 domain cooperates with the MAPK binding linear motif to achieve substrate specific binding, and it also enables co-recruitment of the upstream activating enzyme and the downstream substrate into one signaling competent complex. Studies on present day MAPKs and MKKs hint on the way protein kinase networks may evolve. In particular, they suggest how paralogous enzymes with similar catalytic properties could acquire novel signaling roles by merely changing the way they make physical links to other proteins.
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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.