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Reconstructed ancestral muscle-type acetylcholine receptor β-subunits readily form homopentameric ion channels that open spontaneously, and display functional hallmarks of the modern-day heteropentameric receptor despite being devoid of canonical agonist-binding sites.

Cryo-EM and functional studies reveal how combined action of proteins RPS26/eS26 and RIO1 allows late precursors to the human small ribosomal particle to be matured into fully translation-competent 40S subunits.

The GIRK1 subunit contains a defective Na⁺-binding site but behaves as if it is permanently bound to a sodium ion, and therefore increases the affinity of Gβγ to GIRK1/4 hetero-tetrameric channels in lipid membranes.

In fusion-positive rhabdomyosarcoma, CHD4 positively regulates super-enhancer-mediated gene expression by allowing a chromatin architecture at these cis-regulatory regions, which is permissive to the binding of the transcription factor PAX3-FOXO1.

By linking export and licensing of a piRNA precursor transcript, channel nuclear pore complex subunits Nup54 and Nup58 are specifically required to silence transposons in the Drosophila ovary.

A striking and consequential conductance in vestibular type I hair cells is finally shown to depend on a little-known Shaker subunit that contributes to conventional conductances in other hair cells.

Regulation of Cav2.3 Ca²⁺ channels by membrane-bound β2 subunit splice variants permits long-lasting channel activity even during prolonged and continuous activity in dopamine neurons, with implications for Parkinson's disease pathophysiology.

A cryo-electron microscopy structure of a substrate-bound Vps4-Vta1 AAA ATPase reveals an asymmetric hexameric ring and suggests how nucleotide-induced changes in subunit interfaces translocate polypeptides into the central pore.

A phylum-specific ATP synthase subunit is needed for proper mitochondrial function and stability of the complex in Toxoplasma gondii.

The structure of the human BBSome explains how the subunits interact with each other and how disease-causing mutations hamper this interaction.