Proximity-labeling using engineered biotin ligases TurboID and miniTurbo enables detection of cell-type-specific and low abundance protein complexes and subcellular proteomes in Arabidopsis and other plants.

A proximity labeling approach defines germ granule proteome in Caenorhabditis elegans, and identifies LOTUS domain proteins as key regulators of germ granule assembly.

BLITZ system enables proximity-dependent biotin labelling in live zebrafish embryos with cell and tissue specificity, providing a versatile and valuable tool for proteomic discovery using the zebrafish model.

Proximity biotinylation of the Drosophila centromere suggests a role of RNA helicases, centromeric transcripts, and centromeric R-loops for centromere function.

Proximity labeling-based proteomic strategies applied in zebrafish identify new insights into protein network changes in heart muscle cells during regeneration and implicate Rho A as a target of ErbB2 signaling during zebrafish heart regeneration.

Proteins that are low abundant and/or poorly accessible to antibodies can be readily localised with fluorescent streptavidin, when expressed fused to a biotin ligase.

The molecular microenvironment of coronaviral replicase complexes provides functional and spatial links between conserved cellular processes and viral RNA synthesis, and highlights potential targets for the development of novel antivirals.

Proximity labeling combined with mass spectrometry enables to map the proteasome proximal proteome in cells and mouse tissues.

APEX2 proximity labeling of genetically targeted neurons enables subcellular and cell type-specific proteomics in the mouse brain, revealing the axonal and somatodendritic proteomes of midbrain dopaminergic neurons.

Genetic and proteomic analyses reveal that the SPARK kinase, which is a regulator of key life-cycle transitions in the parasite Toxoplasma gondii, complexes with an elongin-like protein to regulate several important AGC-family kinases.