A post-lysosomal cholesterol transport inhibitor reveals how the endoplasmic reticulum membrane regulates total cellular cholesterol by constantly monitoring a critical pool of cholesterol in the plasma membrane.

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.

Cytotoxicity associated with APOL1 renal-risk variants occurs through its plasma-membrane localization, where aberrant channel activity drives a sustained sodium and calcium influx leading to cell swelling and eventually cell death.

Biochemical and instrumental analysis showed that the membrane-induced exposure of myristoyl from the MA protein of Mason-Pfizer monkey virus triggers allosteric conformational changes resulting in MA oligomerization and unfolding of the cleavage site between MA and downstream domains of Gag.

Plasma membrane damage causes the release of exosomes from cultured human cells.

SAC9 prevents the accumulation of PI(4,5)P₂ in intracellular compartments, thereby contributing to clathrin-mediated endocytosis at the plasma membrane and regulating the cortical localization of its protein partner SH3P2.

We challenge a recent report that most of the cholesterol in the plasma membrane of mammalian cells is in the exofacial leaflet.

Although genetically and biochemically linked, the plant immune and growth receptors FLS2 and BRI1 form dispersed receptor clusters within the plasma membrane that are spatiotemporally separated.

A newly established reversible model of membrane departitioning and repartitioning in bacteria uncovers the role of a cell wall synthase in regulating membrane partitioning.

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