Membrane Trafficking in the Yeast Saccharomyces cerevisiae Model

Abstract

The yeast Saccharomyces cerevisiae is one of the best characterized eukaryotic models. The secretory pathway was the first trafficking pathway clearly understood mainly thanks to the work done in the laboratory of Randy Schekman in the 1980s. They have isolated yeast sec mutants unable to secrete an extracellular enzyme and these SEC genes were identified as encoding key effectors of the secretory machinery. For this work, the 2013 Nobel Prize in Physiology and Medicine has been awarded to Randy Schekman; the prize is shared with James Rothman and Thomas Südhof. Here, we present the different trafficking pathways of yeast S. cerevisiae. At the Golgi apparatus newly synthesized proteins are sorted between those transported to the plasma membrane (PM), or the external medium, via the exocytosis or secretory pathway (SEC), and those targeted to the vacuole either through endosomes (vacuolar protein sorting or VPS pathway) or directly (alkaline phosphatase or ALP pathway). Plasma membrane proteins can be internalized by endocytosis (END) and transported to endosomes where they are sorted between those targeted for vacuolar degradation and those redirected to the Golgi (recycling or RCY pathway). Studies in yeast S. cerevisiae allowed the identification of most of the known effectors, protein complexes, and trafficking pathways in eukaryotic cells, and most of them are conserved among eukaryotes.

Disruption of genes involved in CORVET complex leads to enhanced secretion of heterologous carboxylesterase only in protease deficient Pichia pastoris

“…Disruption of genes involved in CORVET complex leads to enhanced secretion of heterologous carboxylesterase only in protease deficient Pichia pastoris by [4,5]). Heterologous proteins destined for secretion follow the same secretion route.…”

“…In order to be secreted in eukaryotic cells, a protein has to enter the endoplasmic reticulum (ER) lumen where secretory proteins are glycosylated and correctly folded with the help of chaperones and foldases. When the protein is properly folded, it is allowed to be transported to the Golgi apparatus from which it either travels to the cell membrane for secretion or to other cellular compartments such as the vacuole or the endosomes (recently reviewed by ). Heterologous proteins destined for secretion follow the same secretion route.…”

Hygromycin B hypersensitive (hhy) mutants implicate an intact trans-Golgi and late endosome interface in efficient Tor1 vacuolar localization and TORC1 function

“…The vacuole of Saccharomyces cerevisiae is analogous to the mammalian lysosome. Both organelles carry out vital cellular functions including macromolecule degradation, receptor down-regulation, autophagy, and stress survival responses (Bowers and Stevens, 2005; Ostrowicz et al 2008; Veses et al 2008; Li and Kane 2009; Armstrong 2010; Richards et al 2012; Hecht et al 2014; Klionsky and Eskelinen 2014; Feyder et al 2015). We recently performed a genomic screen of the yeast haploid deletion strain collection of non-essential genes for hypersensitivity to hygromycin B ( hhy ) mutants; the small collection of hhy mutants are presented in Table 1 and all were shown to have defects in vacuolar trafficking, morphology and/or stress survival function (Banuelos et al 2010).…”

The wide‐ranging phenotypes of ergosterol biosynthesis mutants, and implications for microbial cell factories

“…There are multiple vesicular trafficking pathways in yeast, which deliver proteins and other compounds between cellular compartments (reviewed inFeyder, De Craene, Bär, Bertazzi, & Friant, 2015). Proteins synthesized at the ER are trafficked via membrane-bound vesicles to the Golgi apparatus.…”