cryo-EM reveals the properties of distinct conformations occupied during activation of the lipid scramblase nhTMEM16 and provides new insights into its interactions with the lipid environment.

Conformational changes occur within extracellular domain of BCR upon antigen engagement, and these conformational changes are related with the strength of BCR activation and are distinct in IgM- and IgG-BCR.

Building on previous work (Tang et al., 2015), novel ESCRT-III subunit Snf7 auto-activation mutants are used to reveal two parallel ubiquitin-dependent pathways during multivesicular endosome biogenesis.

Interleukin 4 signaling co-opts the Akt-mTORC1-Acly pathway to couple metabolic input to the control of energetically demanding processes during macrophage M2 activation.

The Frank–Starling law of the heart and its underlying mechanism of length-dependent activation involve distinctive structural changes in both the thin and thick filaments of cardiac muscle cells.

MLL4 (KMT2D) is a major mammalian H3K4 mono- and di-methyltransferase that is essential for enhancer activation, cell-type-specific gene expression, and cell differentiation.

Activation of CaMKII holoenzymes triggers the exchange of subunits with other holoenzymes, including unactivated ones, enabling the calcium-independent phosphorylation and activation of new subunits.

Activation of Notch receptors by ligands in the same cell (cis-activation) is a prevalent and functional mode of signaling in the Notch pathway, and co-exists with trans-activation and cis-inhibition.

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