The secretory pathway: exploring yeast diversity. Issue 6 (12th April 2013)
- Record Type:
- Journal Article
- Title:
- The secretory pathway: exploring yeast diversity. Issue 6 (12th April 2013)
- Main Title:
- The secretory pathway: exploring yeast diversity
- Authors:
- Delic, Marizela
Valli, Minoska
Graf, Alexandra B.
Pfeffer, Martin
Mattanovich, Diethard
Gasser, Brigitte - Abstract:
- <abstract abstract-type="main" id="fmr12020-abs-0001"> <title>Abstract</title> <p>Protein secretion is an essential process for living organisms. In eukaryotes, this encompasses numerous steps mediated by several hundred cellular proteins. The core functions of translocation through the endoplasmic reticulum membrane, primary glycosylation, folding and quality control, and vesicle‐mediated secretion are similar from yeasts to higher eukaryotes. However, recent research has revealed significant functional differences between yeasts and mammalian cells, and even among diverse yeast species. This review provides a current overview of the canonical protein secretion pathway in the model yeast <italic>Saccharomyces cerevisiae</italic>, highlighting differences to mammalian cells as well as currently unresolved questions, and provides a genomic comparison of the <italic>S. cerevisiae</italic> pathway to seven other yeast species where secretion has been investigated due to their attraction as protein production platforms, or for their relevance as pathogens. The analysis of <italic>Candida albicans</italic>, <italic> Candida glabrata</italic>, <italic> Kluyveromyces lactis</italic>, <italic> Pichia pastoris</italic>, <italic> Hansenula polymorpha</italic>, <italic> Yarrowia lipolytica</italic>, and <italic>Schizosaccharomyces pombe</italic> reveals that many – but not all – secretion steps are more redundant in <italic>S. cerevisiae</italic> due to duplicated genes, while some<abstract abstract-type="main" id="fmr12020-abs-0001"> <title>Abstract</title> <p>Protein secretion is an essential process for living organisms. In eukaryotes, this encompasses numerous steps mediated by several hundred cellular proteins. The core functions of translocation through the endoplasmic reticulum membrane, primary glycosylation, folding and quality control, and vesicle‐mediated secretion are similar from yeasts to higher eukaryotes. However, recent research has revealed significant functional differences between yeasts and mammalian cells, and even among diverse yeast species. This review provides a current overview of the canonical protein secretion pathway in the model yeast <italic>Saccharomyces cerevisiae</italic>, highlighting differences to mammalian cells as well as currently unresolved questions, and provides a genomic comparison of the <italic>S. cerevisiae</italic> pathway to seven other yeast species where secretion has been investigated due to their attraction as protein production platforms, or for their relevance as pathogens. The analysis of <italic>Candida albicans</italic>, <italic> Candida glabrata</italic>, <italic> Kluyveromyces lactis</italic>, <italic> Pichia pastoris</italic>, <italic> Hansenula polymorpha</italic>, <italic> Yarrowia lipolytica</italic>, and <italic>Schizosaccharomyces pombe</italic> reveals that many – but not all – secretion steps are more redundant in <italic>S. cerevisiae</italic> due to duplicated genes, while some processes are even absent in this model yeast. Recent research obviates that even where homologous genes are present, small differences in protein sequence and/or differences in the regulation of gene expression may lead to quite different protein secretion phenotypes.</p> </abstract> … (more)
- Is Part Of:
- FEMS microbiology reviews. Volume 37:Issue 6(2013)
- Journal:
- FEMS microbiology reviews
- Issue:
- Volume 37:Issue 6(2013)
- Issue Display:
- Volume 37, Issue 6 (2013)
- Year:
- 2013
- Volume:
- 37
- Issue:
- 6
- Issue Sort Value:
- 2013-0037-0006-0000
- Page Start:
- 872
- Page End:
- 914
- Publication Date:
- 2013-04-12
- Subjects:
- Microbiology -- Reviews -- Periodicals
Microbiology -- Periodicals
579.05 - Journal URLs:
- http://sciencedirect.com/science/journal/01686445 ↗
http://www.blackwell-synergy.com/rd.asp?goto=journal&code=fmr ↗
http://www3.interscience.wiley.com/journal/118494448/home ↗
http://onlinelibrary.wiley.com/ ↗
http://femsre.oxfordjournals.org/content/ ↗ - DOI:
- 10.1111/1574-6976.12020 ↗
- Languages:
- English
- ISSNs:
- 0168-6445
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.305000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3021.xml