An integrative structural biology approach provides refined models of the KCNQ1-KCNE1 channel complex, which propose a new mechanism to explain how KCNE1 modulates KCNQ1 channel activation.
A combined FRET- and electrophysiology-based approach is used to study ATP/ADP ADP binding to the stimulatory nucleotide binding site of ATP-sensitive K+ channels and investigate their activation mechanism.
Contrary to previous findings, class A GPCRs share a common activation pathway that directly links ligand binding to G-protein activation, as revealed by novel quantitative analysis.
Closed-ring and open-spiral assembly of the multi-subunit neuronal kinase CaMKII suggest a mechanism for how active subunits shuttle between individual assemblies, propagating stimulatory signals.
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.