AirID provides highly interaction-dependent biotinylation for analysis of protein–protein interaction.

Relocation of Rab, Ras and Rho family GTPases to the surface of mitochondria enables efficient identification of their effectors, exchange factors and GAPs by proximity biotinylation.

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

Cohesin adopts a flexible butterfly conformation in vivo and forms spatial and temporal regulated ordered clusters to maintain cohesion and condensation.

One minute biotinylation with APEX2 peroxidase in living cells identifies established and new components of mitochondrial and ER membranes; dataset intersection and overexpression screen identifies SYNJ2BP overexpression as inducing mitochondria-rough ER contacts.

Par3 is polarized in the plane of the vertebrate neural plate, binds and recruits Prickle3 to the apical membrane and promotes the formation of core planar cell polarity complexes.

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

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.

Apicomplexan parasites secrete proteins to manipulate their hosts from sub-apical openings in their cell pellicle that are distinct from the apical complex from where invasion factors are secreted.

A new mass spectrometry-based method to identify and quantify changes in a subcellular local protein environment shows the impact of deletion of a kinase the human malaria parasites export into the host cell.