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Showing 1–8 of 8 results
Advanced filters: Author: Lung-Yu Liang Clear advanced filters

  • The viral Protein Kinase-1 (PK-1) phosphorylates the regulatory protein p6.9, which facilitates baculoviral genome release. Here, the authors combine X-ray crystallography with biophysical and biochemical analyses as well as molecular dynamics simulations to characterize Cydia pomenella granulovirus PK-1, which forms a dimer with a parallel side-to-side arrangement of the kinase domains and furthermore, they provide insights into its catalytic mechanism and evolutionary relationships with other kinases.

    • Michael R. Oliver
    • Christopher R. Horne
    • James M. Murphy
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11

  • The PEAK family of pseudokinases are key hubs in cellular signalling, including cell motility and cancer. Here, the authors characterise how PEAK proteins interact with the adapter proteins CrkII and Grb2 and regulatory scaffold protein 14-3-3, to achieve functional signalling assemblies.

    • Michael J. Roy
    • Minglyanna G. Surudoi
    • Isabelle S. Lucet
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • The necroptotic cell death pathway involves signaling through pseudokinases. Here the authors define the structural determinants of species specificity in necroptosis signaling mediated by the essential necroptotic effector pseudokinase, Mixed Lineage Kinase Domain-Like (MLKL).

    • Katherine A. Davies
    • Cheree Fitzgibbon
    • James M. Murphy
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Necroptosis is a form of cell death characterized by membrane rupture via MLKL oligomerization, although mechanistic details remain unclear. Here, the authors show that MLKL ubiquitylation of K219 facilitates high-order membrane assembly and subsequent rupture, promoting cytotoxicity.

    • Laura Ramos Garcia
    • Tencho Tenev
    • Pascal Meier
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-18

  • The pseudokinase MLKL is activated by the upstream kinase RIPK3 in the necroptotic pathway but the structural basis of MLKL activation is not well understood yet. Here, the authors present the crystal structures of the human RIPK3:MLKL complex and human RIPK3 kinase alone, which reveal structural differences between human and murine RIPK3 and they discuss mechanistic implications.

    • Yanxiang Meng
    • Katherine A. Davies
    • James M. Murphy
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15

  • RIPK3-mediated phosphorylation of the mixed lineage kinase domain-like (MLKL) pseudokinase is thought to be the trigger for MLKL activation during necroptotic signaling. Here the authors provide evidence that the transition of human MLKL from a monomeric state to a tetramer is essential for necroptosis signalling.

    • Emma J. Petrie
    • Jarrod J. Sandow
    • James M. Murphy
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-15

  • This study demonstrates that co-clustering of the EphB6 receptor tyrosine pseudokinase with its ephrinB1 ligand on neighboring cells promotes formation of intercellular tubules. This stabilizes cell-cell adhesion and reduces cancer cell invasion.

    • Lung-Yu Liang
    • Niall D. Geoghegan
    • Isabelle S. Lucet
    ResearchOpen Access
    Communications Biology
    Volume: 7, P: 1-13