title: Governance of endocytic trafficking and signaling by reversible ubiquitylation.
abstract: The endosomal pathway provides a major platform for ubiquitin-modifying enzymes, which act upon membrane-associated proteins in transit. Ubiquitylated cargo proteins are recognized by ubiquitin-binding domains inherent to key adaptor proteins at the plasma membrane and sorting endosome. A balance between ubiquitylation and deubiquitylation activities may govern the efficiency of recycling from endosomes to the plasma membrane versus lysosomal sorting through the multivesicular body pathway. We discuss the current knowledge of the properties of adaptors and ubiquitin-modifying proteins and their effects upon the trafficking and signaling of receptors and ligands associated with pathways fundamental to development.
authors.affiliation: Physiological Laboratory, Institute for Translational Research, University of Liverpool, Crown Street, L69 3BX Liverpool, UK. clague@liv.ac.uk
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Clague
authors.forename: Han
authors.initials: H
authors.lastname: Liu
authors.forename: Sylvie
authors.initials: S
authors.lastname: Urbé
mesh_terms: D000818:Animals; D004705:Endocytosis; D011992:Endosomes / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D015398:Signal Transduction; D025801:Ubiquitin / Q000378:metabolism*; D043743:Ubiquitin-Protein Ligase Complexes / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D025801:Ubiquitin; D043743:Ubiquitin-Protein Ligase Complexes