Msp1, a membrane-integral AAA ATPase at mitochondria and peroxisomes, selectively recognizes uncomplexed substrate molecules in vivo while avoiding substrates stabilized by binding partners.

Biochemical dissections show that the Guided Entry of Tail Anchored proteins (GET) pathway selects ER-destined tail-anchored proteins using at least two distinct molecular mechanisms, each recognizing a distinct physicochemical feature in the substrate.

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.

HiLITR is a molecular reporter of protein localization that enables straightforward, large-scale, fluorescence-activated cell sorting-based discovery of genes that regulate complex cellular processes, such as mitochondrial and ER tail-anchored protein trafficking.

Using a suite of CRISPR technologies, unique chemical tools, and carefully designed biochemical and cell biological assays, we define the mechanism of action of Retro-2, an inhibitor of retrograde toxins.

Msp1 recruits substrates at the open seam of the spiral oligomer and extracts them with functionally adapted elements.

Genome-wide recruitment of Mediator and Pol II is reduced in yeast lacking the Med2-Med3-Med15 tail module triad, and Mediator association with gene promoters depends on Pol II, Taf1, and TBP.

Posterior determination of Drosophila oocyte is defined by competition between kinesin-1 removing posterior determinants from the cortex and myosin-V anchoring them.

Stromules induced during plant innate immunity dynamically interact and use the cytoskeleton to form and to direct the movement of chloroplasts.

Emerin, a protein that plays key roles in nuclear organization, can be dynamically degraded in response to environmental stimuli such as ER stress.