title: Yarrowia lipolytica vesicle-mediated protein transport pathways.
abstract: BACKGROUND
  Protein secretion is a universal cellular process involving vesicles which bud and fuse between organelles to bring proteins to their final destination. Vesicle budding is mediated by protein coats; vesicle targeting and fusion depend on Rab GTPase, tethering factors and SNARE complexes. The Génolevures II sequencing project made available entire genome sequences of four hemiascomycetous yeasts, Yarrowia lipolytica, Debaryomyces hansenii, Kluyveromyces lactis and Candida glabrata. Y. lipolytica is a dimorphic yeast and has good capacities to secrete proteins. The translocation of nascent protein through the endoplasmic reticulum membrane was well studied in Y. lipolytica and is largely co-translational as in the mammalian protein secretion pathway.
  
  
  RESULTS
  We identified S. cerevisiae proteins involved in vesicular secretion and these protein sequences were used for the BLAST searches against Génolevures protein database (Y. lipolytica, C. glabrata, K. lactis and D. hansenii). These proteins are well conserved between these yeasts and Saccharomyces cerevisiae. We note several specificities of Y. lipolytica which may be related to its good protein secretion capacities and to its dimorphic aspect. An expansion of the Y. lipolytica Rab protein family was observed with autoBLAST and the Rab2- and Rab4-related members were identified with BLAST against NCBI protein database. An expansion of this family is also found in filamentous fungi and may reflect the greater complexity of the Y. lipolytica secretion pathway. The Rab4p-related protein may play a role in membrane recycling as rab4 deleted strain shows a modification of colony morphology, dimorphic transition and permeability. Similarly, we find three copies of the gene (SSO) encoding the plasma membrane SNARE protein. Quantification of the percentages of proteins with the greatest homology between S. cerevisiae, Y. lipolytica and animal homologues involved in vesicular transport shows that 40% of Y. lipolytica proteins are closer to animal ones, whereas they are only 13% in the case of S. cerevisiae.
  
  
  CONCLUSIONS
  These results provide further support for the idea, previously noted about the endoplasmic reticulum translocation pathway, that Y. lipolytica is more representative of vesicular secretion of animals and other fungi than is S. cerevisiae.
authors.affiliation: Laboratoire de Microbiologie et Génétique Moléculaire INRA-CNRS-AgroParisTech UMR 1238 CBAI BP01 F-78850 Thiverval Grignon, France. dominique.swennen@grignon.inra.fr
authors.forename: Dominique
authors.initials: D
authors.lastname: Swennen
authors.forename: Jean-Marie
authors.initials: JM
authors.lastname: Beckerich
mesh_terms: D000595:Amino Acid Sequence; D001692:Biological Transport; D019295:Computational Biology; D005656:Fungal Proteins / Q000378:metabolism*; D010802:Phylogeny; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D016415:Sequence Alignment; D033921:Vesicular Transport Proteins / Q000378:metabolism*; D025062:Yarrowia / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins