Defective mitochondrial protein import results in protein aggregation and a specific chaperone response in the cytosol, causatively linking mitochondrial function and cellular protein homeostasis disturbances observed in neurodegeneration.

An array of cytosolic co-chaperones and chaperones helps to maintain newly synthesized mitochondrial outer membrane proteins in an import competent state.

Cytosolic S100A8/A9 enhances Ca²⁺ availability at LFA-1 adhesion sites, facilitating neutrophil recruitment and extravasation by supporting proper integrin signaling and cytoskeletal rearrangement.

Identification of a transporter complex comprised of SLC37A3 and ATRAID is required for nitrogen-containing bisphosphonates to enter the cytosol from lysosomes and exert their therapeutic effects on bone.

In the cytosol, the proteins constituting cell-matrix adhesion sites form multi-protein building blocks which enter and leave these sites unaltered, thereby contributing to their rapid and correct self-assembly.

Stramenopiles are unusual, because the pay-off phase of glycolysis occurs in mitochondria rather than the cytosol and the identified mitochondrial carrier links the two parts by transporting glycolytic intermediates.

The damage of the bacterial cell envelope is found to be only a secondary effect of the antimicrobial activity of lactoferricin derivatives.

The C2-domain of cytoplasmic phospholipase A₂α is structurally designed to target PC-rich membrane regions to increase the enzymatic efficiency of the catalytic domain, which prefers PCs with polyunsaturated acyl chains.

Live-cell nanometer-resolution RNA labeling method enables transcriptome-wide mapping of endogenous RNAs in nuclear, cytosol, ER, and mitochondrial subcompartments.

A new unfolded protein response has been discovered that is distinct from the heat shock response and protects mammalian cells from proteotoxic stress.