The ability of epithelial cells to distinguish between domains on opposing cell surfaces within a tissue, a property known as planar cell polarity, relies on proteins and protein complexes directing the traffic of signaling proteins to specific locations on the cell surface membrane.

A single transmembrane E3 ligase complex can regulate protein ubiquitination at multiple organelles using interchangeable targeting subunits.

GnT1IP-L is a membrane bound glycoprotein that interacts with MGAT1 in the Golgi, but not in the endoplasmic reticulum, to regulate complex N-glycan synthesis.

Association of curvature generating proteins to the Golgi membranes by sphingomyelin metabolism essentially controls the flatness of a Golgi cisterna that is necessary for efficient sorting and export.

The soluble cargo protein albumin traverses the Golgi stack at much faster rates than procollagen aggregates, by diffusion via intercisternal continuities.

Atomic force microscopy reveals a floppy, dimeric, coiled coil Golgin structure that captures transport vesicles via splayed, N-terminal ends at the Golgi complex.

Transmembrane protein Erd1 and the cytosolic receptor Vps74 cooperate to mediate early Golgi glycosyltransferase recycling in budding yeast.

Imaging, quantitative immunoblotting and mass spectrometry reveal that hundreds of surface-expressed neuronal membrane proteins exhibit atypical glycosylation profiles, resulting in changes in protein half-life and synaptic responses.

A mathematical model of glycosylation in the Golgi apparatus to investigate how the fidelity of synthesising a complex glycan distribution at the plasma membrane depends on parameters such as the number of Golgi cisternae or enzyme specificity.

Rab6A binds directly to both the C-terminus and the N-terminal motor domain of the kinesin KIF1C to regulate vesicle motility and Golgi organization.