Single molecule microscopy combined with biochemical analyses show that a two-step lipid-binding mechanism of the SRP receptor balances the trade-off between speed and specificity during co-translational protein targeting.
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.
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.
Structures of the signal recognition particle before and after it captures a transmembrane domain suggest how it chooses, engages, and shields its clients during membrane protein targeting to the endoplasmic reticulum.
Proteomics and functional genomics coupled to an antibody discovery pipeline revealed the influence of oncogenic RAS signaling on the cell-surface proteome and resulted in the discovery of potential therapeutic targets for RAS-driven cancers.
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.
During centrosome maturation, pericentrin is delivered to the centrosome co-translationally by a microtubule- and dynein-dependent process, as pericentrin mRNA is undergoing active translation near the centrosome.