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 Rag-family GTPases, known activators of TOR complex 1 (TORC1), also function as attenuator that prevents deregulated hyperactivation of TORC1 signaling.

A critical second step in DNA tethering by cohesin occurs after its stable binding to DNA, and this second step is modulated by the Smc3 ATPase active site in Saccharomyces cerevisiae.

A small GTPase within the flagellum can participate in the control of transport from the base to the tip of the flagellum, and back again.

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

The H+ influx coupled to nutrient uptake and the plasma membrane H+-ATPase are central actors of the activation of target of rapamycin complex 1 (TORC1) in budding yeast Saccharomyces cerevisiae..

The cryo-electron microscopy structure of an assembly of the WAVE Regulatory Complex and its activator, the Rac GTPase, plus complementary biochemistry and biophysics, reveal a novel activation mechanism involving two distinct Rac binding sites.

The human Origin Replication Complex is shaped as a shallow corkscrew in a classic AAA+ organization reminiscent of clamp loader complexes with highly controlled ATPase activity as exemplified by Meier-Gorlin syndrome mutations.

Genetic labeling of cells that survive executioner caspase activity in Drosophila reveals distinct patterns in different tissues.

An unbiased genome-wide human forward genetic screen identifies the vacuolar ATPase complex and assembly factors as regulators of HIF stability through their actions on intracellular iron metabolism.