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.

Unconventional secretion of a plasma membrane purine transporter via Golgi-bypass is established at an early ER-associated secretory compartment revealing that specific cargoes define alternative trafficking routes.

Neurons use a non-canonical secretory network to deliver select proteins to postsynaptic sites in dendrites.

The ATP7A interactome is the first comprehensive view of putative Menkes disease neurodegeneration mechanisms.

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

Uso1 critically regulating traffic in the ER/Golgi interface is a coiled-coil protein traditionally regarded as a tether, but a forward genetic screen revealed that its essential role appears to involve its ability to interact with SNAREs.

The glycinergic neurons of the cerebellar nuclei project extensively to the cerebellar cortex and inhibit GABAergic Golgi cells.

Evidence that certain proteins can be transported between Golgi via structures that resemble COPI vesicles suggests that these vesicles could also be involved in the transport of proteins from the cis to the trans face of the Golgi.

Direct measurements of trafficking kinetics between organelles of the secretory pathway suggest that lipid-driven membrane domains laterally sort proteins during membrane traffic.