Scientists have long sought a robust picture of how the Golgi complex, an organelle critical to the post-translational modification and sorting of newly synthesized proteins, operates. The Golgi contains multiple subcompartments—cis (early), medial (middle) and trans (late) cisternae—each housing different sets of glycosyltransferases and other enzymes. Proteins enter the Golgi at the cis compartment and exit at the trans compartment, but how they move from one cisterna to the next is still somewhat mysterious.
Now, recent findings are helping to resolve the issue.
One model for membrane traffic within the Golgi apparatus has led the pack.1 According to the cisternal maturation (or progression) model, cargo remains in a given compartment and different enzymes arrive there, to convert a cis cisterna into a medial one, or a medial cisterna into a trans cisterna. Researchers have already determined this type of maturation to be at play in endocytosis.2 On endosomes, small Rab ...