Segregation in the Golgi complex precedes export of endolysosomal proteins in distinct transport carriers.

ABSTRACT: Biosynthetic sorting of newly synthesized transmembrane cargos to endosomes and lysosomes is thought to occur at the TGN through recognition of sorting signals in the cytosolic tails of the cargos by adaptor proteins, leading to cargo packaging into coated vesicles destined for the endolysosomal system. Here we present evidence for a different mechanism in which two sets of endolysosomal proteins undergo early segregation to distinct domains of the Golgi complex by virtue of the proteins' luminal and transmembrane domains. Proteins in one Golgi domain exit into predominantly vesicular carriers by interaction of sorting signals with adaptor proteins, but proteins in the other domain exit into predominantly tubular carriers shared with plasma membrane proteins, independently of signal-adapto

SUBMITTER: Chen Y 

PROVIDER: S-EPMC5716290 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature