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

Cryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H⁺ translocation in the V_o membrane domain.

Sec14l3/SEC14L2 respond to upstream Wnt/Frizzled/Dvl stimulation to recruit and activate phospholipase Cδ4a (Plcδ4a) to further initiate calcium release.

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.

The chaperone protein BiP forms complexes with Ire1 and Perk that dissociate when unfolded proteins bind to BiP to activate the unfolded protein response in the ER.

Intravascular triglyceride hydrolysis by lipoprotein lipase is crucial for delivering lipid nutrients to vital tissues, such as the heart, skeletal muscle, and adipose tissue.

The ATPase Fap7 prefabricates a uS11:eS26 ribosomal protein complex for ribosome assembly.

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.

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.

The ATPase Dhh1 controls processing body formation and disassembly in yeast cells, and processing body dynamics can be recapitulated in vitro with recombinant Dhh1, ATP and RNA.