Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.

A 3.2 Å resolution structure of Vps4 provides a detailed model for protein substrate binding and translocation by AAA ATPases.

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.

Cryo-EM reveals the regulation of RUVBL1 and RUVBL2 AAA-ATPases by DHX34, a helicase involved in nonsense-mediated mRNA decay (NMD), and suggests mechanisms for how RUVBL1 and RUVBL2 function in NMD.

TRIP13 inactivates the spindle assembly checkpoint by converting MAD2 from its active ‘closed’ state to its inactive ‘open’ state.

High resolution structures of the essential human AAA+ ATPase TorsinA and its disease mutant in complex with an activator reveal details of the interaction that will guide drug design and further functional characterization.

LAP1 adopts an AAA+ like fold that, while unable to bind nucleotide, can enhance ATPase activity in the neighboring TorsinA protomer in an unusual heterohexameric ring, via an arginine finger.

Multicellular and socially aggregating prokaryotes contain previously undescribed, chaperone-based systems predicted to mediate defensive biological conflicts, several components of which are thematically similar antecedents of eukaryotic apoptosis pathways.

The structure of a substrate-engaged AAA+ unfoldase suggests a model for processive unfolding that is supported by biochemical data.

Structure-guided biochemistry defines how the coupling between nucleic acid substrate binding and ATPase activity is used by a molecular switch to load ring-shaped motor proteins onto single-stranded DNA.