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.

The golgin GMAP-210 captures vesicles at the cis Golgi by merely recognizing the high curvature and lipid unsaturation level of transport vesicles.

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.

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.

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

The cisternae of the Golgi contain two functionally distinct domains: the central areas, which remain stationary, and the edges or rims, which are mobile.

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.

Inactivation of the COPI vesicle coat in yeast reveals that COPI recycles early but not late Golgi proteins.

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.