Doa10, a membrane-embedded ubiquitin ligase, facilitates the removal of membrane proteins from the endoplasmic reticulum and cooperates with the Cdc48 ATPase in this process.

Coarse-grained modeling reveals a new mechanism for multispanning membrane protein topogenesis, in which misintegrated configurations of the proteins undergo post-translational annealing to reach final, fully integrated multispanning topologies.

Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.

A simple, yet elegant method for robust self-assembly of diverse membrane proteins into soluble peptide nanoparticles for their structural and functional analysis in detergent-free solutions.

A new family of sterol-specific lipid transfer proteins has been found that anchors in the endoplasmic reticulum; some of these proteins stretch across membrane contacts and mediate sterol traffic from the plasma membrane.

During cilium-generated signaling, ciliary membrane protein trafficking is unidirectional and ciliary membrane protein composition is regulated through action in the cytoplasm of the retrograde intraflagelllar transport (IFT) motor and shedding of ciliary ectosomes.

Translation pauses occur in strategic positions to facilitate the production of properly folded membrane proteins in bacteria.

A set of ER-localized membrane proteins whose loss causes developmental diseases in humans, assemble with Sec61 into a translocon that facilitates the biogenesis of hundreds of different multi-pass membrane proteins.

A facile method is implemented to modify membrane proteins with biophysical reporters using cysteine-independent approaches in live cells.

A structure of the complete, membrane bound, COPII coat solved by sub-tomogram averaging reveals the arrangement of all protein subunits on the membrane and suggests a mechanism for coating heterogeneously-shaped carriers.