High-throughput analysis of several Saccharomyces cerevisiae contact sites reveals a large data set of potential contact site proteins, including proteins involved in the regulation of lipid distribution within cells.

Depletion of VAPA in cancer cells induces defects in actin organization, adhesion dynamics and cell migration, together with a perturbation of phosphoinositide levels at the plasma membrane and a lack of anchoring of ER-PM contact sites to focal adhesions.

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

Increasing endoplasmic reticulum (ER)–mitochondria contact sites leads to neurodegeneration.

A mechanosensitive ion channel physically and genetically interacts with proteins that function at endoplasmic reticulum–plasma membrane contact sites.

Sphingolipids regulate vacuolar fission via nuclear vacuole junction to adapt to intracellular and extracellular environments in budding yeast.

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.

To establish membrane contacts between its vacuole and the endoplasmic reticulum, the obligate intracellular bacterial pathogen Chlamydia trachomatis has evolved complex molecular strategies to mimic emerging regulatory processes that control contact-dependent organelle–organelle communication.

Oxidative stress leads to the translocation of Rab5 from endosome to mitochondria, regulated by ALS/Alsin, a component associated with amyotrophic lateral sclerosis, leading to mitochondrial-endosomal physical contacts and a cytoprotective response.

Interactions between Aim24 and the mitochondrial outer and inner membrane contact site complex (MICOS) are essential for mitochondrial ultrastructure, lipid composition and oxidative phosphorylation.