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

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

Building on previous work (Mysling et al., 2016), it is shown that angiopoietin-like protein 4 (ANGPTL4) inhibits lipoprotein lipase activity by catalyzing the unfolding of its hydrolase domain.

Efficient targeting of membrane proteins from the endoplasmic reticulum (ER) to the inner nuclear membrane depends on GTP hydrolysis by Atlastin GTPases and their function in maintaining an interconnected topology of the ER network.

The endoplasmic reticulum E3 ubiquitin ligase Doa10 and the mitochondrial AAA-ATPase Msp1 govern targeting fidelity of outer mitochondrial tail-anchored proteins by controlling cytoplasmic concentration and extracting mistargeted and orphan species.

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

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 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.

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.

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.