title: Clathrin and post-Golgi trafficking: a very complicated issue.
abstract: Clathrin-coated vesicles (CCVs) are formed at the plasma membrane and act as vectors for endocytosis. They also assemble at the trans-Golgi network (TGN), but their exact function at this organelle is unclear. Recent studies have examined the effects on vacuolar and secretory protein transport of knockout mutations of the adaptor protein 1 (AP1) μ-adaptin subunit AP1M, but these investigations do not clarify the situation. These mutations lead to the abrogation of multiple trafficking pathways at the TGN and cannot be used as evidence in favour of CCVs being agents for receptor-mediated export of vacuolar proteins out of the TGN. This transport process could just as easily occur through the maturation of the TGN into intermediate compartments that subsequently fuse with the vacuole.
authors.affiliation: Centre for Organismal Studies (COS), University of Heidelberg, Heidelberg, Germany. Electronic address: david.robinson@urz.uni-heidelberg.de.
authors.forename: David G
authors.initials: DG
authors.lastname: Robinson
authors.affiliation: Center for Plant Molecular Biology (ZMBP), University of Tübingen, Tübingen, Germany.
authors.forename: Peter
authors.initials: P
authors.lastname: Pimpl
mesh_terms: D000818:Animals; D002966:Clathrin / Q000378:metabolism*; D022163:Clathrin-Coated Vesicles / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D006801:Humans; D009154:Mutation; D021601:trans-Golgi Network / Q000378:metabolism
chemical_list: D002966:Clathrin
keywords: TGN maturation; adaptor mutants; clathrin-coated vesicles; vacuolar protein transport