A new insight into the role of syntaxin1's juxtamembrane region in controlling palmitoylation and spontaneous neurotransmitter release.

PTEN organizes multicellular architecture by non-catalytic scaffolding of spatially localized β-Arrestin1/ARHGAP21/Cdc42 protein complexes to control mitotic spindle orientation, multicellular configuration and lumen formation.

Deep mutational scanning reveals interactions in the MET kinase domain that are critical for regulation and cancer-related signaling.

The crystal structures of the intracellular part of the plexin receptor in the active dimer form, and its complex with a key downstream signalling protein Rap, provide insights into how plexin initiates a signalling cascade involved in axon guidance.

Ligand binding to the ectodomain of the insulin-like growth factor receptor destabilises an autoinhibitory inter-subunit interaction, which allows the transmembrane domains to associate and the intracellular regions to autophosphorylate.

An intracellular cytokine receptor 'switch' motif is critical for the dimerization of JAK2 and activation of the JAK2 kinase.

The modularity and unequivocal input/response of Notch signaling are harnessed to measure cell-surface shedding of diverse transmembrane receptors to identify new proteolytic switches and detect modulation of proteolysis by therapeutics.

Ligand binding induces DDR1 kinase activity through recruitment of DDR1 receptors into signalling clusters in which phosphorylation occurs across different dimers.

A model for synchronous neurotransmitter release suggests that when not in the presence of calcium ions, Synaptotagmin proteins form ring-like structures between the vesicle and plasma membrane that prevent spontaneous fusion.

The prolactin receptor, Janus kinase 2, and PI(4,5)P₂ form a co-structure with the membrane resulting in orientations with different accessibility fixing the disordered juxtamembrane domain of the receptor in an extended structure.