Imaging with electron microscopy and cryo-electron tomography reveals that competition between Cdc42 and Gic1 for the same subunit within septins controls the formation and breakdown of septin filaments.

Optogenetic control of Cdc42 activation during polarization of budding yeast demonstrates a cell cycle regulated switch between two distinct modes of positive feedback.

Minimal essential features of Rho GTPase systems are elucidated that regulate the number of distinct domains developed by a cell’s polarity machinery, which in turn governs cell shape.

The scaffold Bem1 increases the rate of GEF-mediated Cdc42 activation, while also increasing the rate and extent of GEF phosphorylation by PAK, which attenuates further scaffold stimulation.

In budding yeast, nascent polarity sites engage in a winner-takes-all contest to determine a single front.

A signaling pathway—comprising a linear sequence of the ubiquitin-selective chaperone Cdc48/p97 and the deubiquitylases Ubp12 and Ubp2—synergistically regulates mitochondrial fusion, thereby fine-tuning ubiquitylation of the mitofusin Fzo1.

The enzyme that collaborates with ubiquitin ligases to promote the release of defective polypeptides from stalled ribosomes in a process named ribosome-associated degradations has been identified as the ATPase Cdc48.

Wss1 is both a metalloprotease and SUMO ligase found in association with Cdc48 and Doa1 and accumulating in the vacuole upon DNA damage.

Conditional knockout of the small GTPase Cdc42 in excitatory neurons of the mouse forebrain leads to impaired long-term synaptic plasticity and impaired retrieval of remote memory.

The SUMO-Ub-Cdc48 pathway is a novel regulatory mechanism of Pol III and a potential therapeutic target for Pol III-related human diseases.