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Sphingolipids govern the compartmentalization of yeast cells through the assembly of lateral diffusion barriers in ER membranes.

Structure-function characterization of the EMC's cytoplasmic, transmembrane, and lumenal domains reveal features critical for terminal helix insertion and a specialized role for the lumenal domain in polytopic membrane protein biogenesis.

The ER transmembrane protein VMP1 is important for release of lipoproteins from the ER membrane into the ER lumen for secretion.

TANGO1 functions as a linactant filament to stabilize shallow COPII-coated buds, and after which membrane tension regulation, possibly mediated by TANGO1-controlled membrane fusion, facilitates bud elongation for procollagen export.

Ubiquitin ligase adaptors target the selective clearance of misfolded plasma membrane proteins.

GRAMD1 proteins sense a transient expansion of the accessible pool of plasma membrane cholesterol and facilitate its transport to the endoplasmic reticulum at ER-PM contact sites.

ABHD16A is a phospholipid-modifying endoplasmic reticulum (ER) membrane protein required for both mitochondrial fission and fusion machinery recruitment to ER-associated mitochondrial constrictions.

Membralin mutant mice manifest a severe and early-onset motor neuron disease with defects in endoplasmic reticulum-associated protein degradation.

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.

Functionally distinct ER-PM domains in human cells are defined by conserved GRAM domain containing proteins.