Open AccessEndosomal trafficking of yeast membrane proteins
Author(s) -
Kamilla M.E. Laidlaw,
Chris MacDonald
Publication year - 2018
Publication title -
biochemical society transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.562
H-Index - 144
eISSN - 1470-8752
pISSN - 0300-5127
DOI - 10.1042/bst20180258
Subject(s) - endosome , escrt , microbiology and biotechnology , lysosome , protein targeting , retromer , transport protein , ubiquitin , saccharomyces cerevisiae , vesicular transport proteins , golgi apparatus , sorting nexin , membrane protein , biology , chemistry , yeast , vacuolar protein sorting , intracellular , membrane , biochemistry , endoplasmic reticulum , gene , enzyme
Various membrane trafficking pathways transport molecules through the endosomal system of eukaryotic cells, where trafficking decisions control the localisation and activity of a diverse repertoire of membrane protein cargoes. The budding yeast Saccharomyces cerevisiae has been used to discover and define many mechanisms that regulate conserved features of endosomal trafficking. Internalised surface membrane proteins first localise to endosomes before sorting to other compartments. Ubiquitination of endosomal membrane proteins is a signal for their degradation. Ubiquitinated cargoes are recognised by the endosomal sorting complex required for transport (ESCRT) apparatus, which mediate sorting through the multivesicular body pathway to the lysosome for degradation. Proteins that are not destined for degradation can be recycled to other intracellular compartments, such as the Golgi and the plasma membrane. In this review, we discuss recent developments elucidating the mechanisms that drive membrane protein degradation and recycling pathways in yeast.