Differential inhibition of multiple vesicular transport steps between the endoplasmic reticulum and trans Golgi network.

TL;DR: The existence of a di-acidic signal on the cytoplasmic tail of vesicular stomatitis virus glycoprotein and other cargo molecules was required for efficient recruitment to vesicles mediating export from the ER in baby hamster kidney cells and provides evidence that exportFrom the ER occurs through a selective mechanism.

TL;DR: It is concluded that budding from the ER through recruitment of COPII is confined to highly specialized export complexes that topologically restrict anterograde transport to regional foci to facilitate efficient coupling to retrograde recycling by COPI.

TL;DR: The central role of ARF1 in controlling vesicular traffic from the endoplasmic reticulum (ER) to the Golgi apparatus and between successive Golgi compartments is demonstrated and it is suggested that ARF and ARF-GEF are essential for export from the ER.

TL;DR: It is proposed that sequential coupling between COPII and COPI coats is essential to coordinate and direct bi-directional vesicular traffic between the ER and pre-Golgi intermediates involved in transport of protein to the Golgi complex.

TL;DR: The title of the Nobel Lecture of George Palade (1 August, p. 347) should have been "Intracellular aspects of the process of protein secretion."

TL;DR: Electron microscopy of sec mutant cells reveals the temperature-dependent accumulation of membrane-enclosed secretory organelles, and it is suggested that these structures represent intermediates in a pathway in which secretion and plasma membrane assembly are colinear.

TL;DR: An enzyme that hydrolyzes di-N-acetylchitobiose linkages in oligosaccharides and glycoproteins was purified to homogeneity from cultural filtrates of Streptomyces griseus and appears to consist of a single polypeptide chain.