ArticleScience signaling2015
Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases.
Article in Science signaling, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
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- Molecular determinants of signal transduction in tropomyosin receptor kinases.FEBS open bio · 2026Review
- Allosteric Coupling in Full-Length Lyn Kinase Revealed by Molecular Dynamics and Network Analysis.International journal of molecular sciences · 2025Article
- Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases.Nature communications · 2024Article
- Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases.Research square · 2024Article
- Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases.bioRxiv : the preprint server for biology · 2024Article
- EGGNet, a Generalizable Geometric Deep Learning Framework for Protein Complex Pose Scoring.ACS omega · 2024Article
- A critical evaluation of protein kinase regulation by activation loop autophosphorylation.eLife · 2023Article
- Unified access to up-to-date residue-level annotations from UniProtKB and other biological databases for PDB data.Scientific data · 2023Article
- Antitumor activity of a lectibody targeting cancer-associated high-mannose glycans.Molecular therapy : the journal of the American Society of Gene Therapy · 2022Article
- PLCγ2 impacts microglia-related effectors revealing variants and pathways important in Alzheimer's disease.Frontiers in cell and developmental biology · 2022Review
- Pondering the mechanism of receptor tyrosine kinase activation: The case for ligand-specific dimer microstate ensembles.Current opinion in structural biology · 2021Review
- CD146 bound to LCK promotes T cell receptor signaling and antitumor immune responses in mice.The Journal of clinical investigation · 2021Article
- Ligand bias in receptor tyrosine kinase signaling.The Journal of biological chemistry · 2020Review
- The biophysical basis of receptor tyrosine kinase ligand functional selectivity: Trk-B case study.The Biochemical journal · 2020Article
- Increasing kinase domain proximity promotes MST2 autophosphorylation during Hippo signaling.The Journal of biological chemistry · 2020Article
- Rh-CSF1 attenuates neuroinflammation via the CSF1R/PLCG2/PKCε pathway in a rat model of neonatal HIE.Journal of neuroinflammation · 2020Article
- ProtCID: a data resource for structural information on protein interactions.Nature communications · 2020Article
- Clinically Precedented Protein Kinases: Rationale for Their Use in Neurodegenerative Disease.Frontiers in aging neuroscience · 2020Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Protein kinase autophosphorylation is a common regulatory mechanism in cell signaling pathways. Crystal structures of several homomeric protein kinase complexes have a serine, threonine, or tyrosine autophosphorylation site of one kinase monomer located in the active site of another monomer, a structural complex that we call an "autophosphorylation complex." We developed and applied a structural bioinformatics method to identify all such autophosphorylation complexes in x-ray crystallographic structures in the Protein Data Bank (PDB). We identified 15 autophosphorylation complexes in the PDB, of which five complexes had not previously been described in the publications describing the crystal structures. These five complexes consist of tyrosine residues in the N-terminal juxtamembrane regions of colony-stimulating factor 1 receptor (CSF1R, Tyr(561)) and ephrin receptor A2 (EPHA2, Tyr(594)), tyrosine residues in the activation loops of the SRC kinase family member LCK (Tyr(394)) and insulin-like growth factor 1 receptor (IGF1R, Tyr(1166)), and a serine in a nuclear localization signal region of CDC-like kinase 2 (CLK2, Ser(142)). Mutations in the complex interface may alter autophosphorylation activity and contribute to disease; therefore, we mutated residues in the autophosphorylation complex interface of LCK and found that two mutations impaired autophosphorylation (T445V and N446A) and mutation of Pro(447) to Ala, Gly, or Leu increased autophosphorylation. The identified autophosphorylation sites are conserved in many kinases, suggesting that, by homology, these complexes may provide insight into autophosphorylation complex interfaces of kinases that are relevant drug targets.
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