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.

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

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.

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.

The life cycle and morphology of the sea squirt Ciona intestinalis shed light on vertebrate evolution.

Guidelines governing research into embryos need to be updated in a way that reflects the moral status of synthetic human entities generated using the methods of synthetic biology.

Tom1 is the ubiquitin ligase in yeast that anchors a protein quality control pathway that rapidly eliminates ribosomal proteins that fail to assemble into ribosomes.

Boundary cell identity and sharpening of borders are coupled in hindbrain development since both are regulated by mechanical tension.