The endoplasmic reticulum (ER) is the site of membrane protein insertion, folding, and
assembly in eukaryotes. Over the past few years, a combination of genetic and biochemical …

Multipass membrane proteins contain two or more α-helical transmembrane domains
(TMDs) that span the lipid bilayer. They are inserted cotranslationally into the prokaryotic …

In the mitochondrial outer membrane, α-helical transmembrane proteins play critical roles in
cytoplasmic-mitochondrial communication. Using genome-wide CRISPR screens, we …

Most eukaryotic multipass membrane proteins are inserted into the membrane of the
endoplasmic reticulum. Their transmembrane domains (TMDs) are thought to be inserted co …

Insertion of proteins into membranes is an essential cellular process. The extensive
biophysical and topological diversity of membrane proteins necessitates multiple insertion …

Most available information on endoplasmic reticulum (ER)-plasma membrane (PM) contacts
in cells of higher eukaryotes concerns proteins implicated in the regulation of Ca 2+ entry …

Hundreds of proteins are anchored in intracellular membranes by a single transmembrane
domain (TMD) close to the C terminus. Although these tail-anchored (TA) proteins serve …

Membrane proteins are inserted into the endoplasmic reticulum (ER) by two highly
conserved parallel pathways. The well-studied co-translational pathway uses signal …

Recent research has provided an abundance of new information on membrane
biochemistry. Now more than ever, it is essential to update our current understanding of …

Approximately 25% of eukaryotic genes code for integral membrane proteins that are
assembled at the endoplasmic reticulum. An abundant and widely conserved multi-protein …