The ER membrane protein complex promotes the biogenesis of a subset multipass membrane proteins enriched for transporters and other proteins with destabilizing features in transmembrane domains.

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

The ER membrane protein complex (EMC) facilitates the correct topology of the flavivirus non-structural proteins NS4A and NS4B at the ER membrane critical for viral replication.

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.

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.

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.

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.

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.

Experiments with mammalian cells and Xenopus egg extracts elucidate how three proteins cooperate to shape the reticular endoplasmic reticulum network.

Biochemical and cell-based analyses reveal how a non-enveloped virus exploits the chaperone activity of an ER transmembrane protein to penetrate the ER membrane required for successful virus infection.