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Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion.
- Source :
-
Eukaryotic cell [Eukaryot Cell] 2012 Aug; Vol. 11 (8), pp. 1075-82. Date of Electronic Publication: 2012 Jun 29. - Publication Year :
- 2012
-
Abstract
- Glycolytic enzymes are cytosolic proteins, but they also play important extracellular roles in cell-cell communication and infection. We used Saccharomyces cerevisiae to analyze the secretory pathway of some of these enzymes, including enolase, phosphoglucose isomerase, triose phosphate isomerase, and fructose 1,6-bisphosphate aldolase. Enolase, phosphoglucose isomerase, and an N-terminal 28-amino-acid-long fragment of enolase were secreted in a sec23-independent manner. The enhanced green fluorescent protein (EGFP)-conjugated enolase fragment formed cellular foci, some of which were found at the cell periphery. Therefore, we speculated that an overview of the secretory pathway could be gained by investigating the colocalization of the enolase fragment with intracellular proteins. The DsRed-conjugated enolase fragment colocalized with membrane proteins at the cis-Golgi complex, nucleus, endosome, and plasma membrane, but not the mitochondria. In addition, the secretion of full-length enolase was inhibited in a knockout mutant of the intracellular SNARE protein-coding gene TLG2. Our results suggest that enolase is secreted via a SNARE-dependent secretory pathway in S. cerevisiae.
- Subjects :
- Cell Membrane chemistry
Endosomes chemistry
Genes, Reporter genetics
Glucose-6-Phosphate Isomerase genetics
Glucose-6-Phosphate Isomerase metabolism
Golgi Apparatus chemistry
Green Fluorescent Proteins genetics
Luminescent Proteins genetics
Mitochondria chemistry
Mutation
Phosphopyruvate Hydratase analysis
Phosphopyruvate Hydratase genetics
Protein Transport
Qa-SNARE Proteins genetics
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae Proteins analysis
Saccharomyces cerevisiae Proteins genetics
Secretory Pathway
Phosphopyruvate Hydratase metabolism
Qa-SNARE Proteins metabolism
Saccharomyces cerevisiae enzymology
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1535-9786
- Volume :
- 11
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Eukaryotic cell
- Publication Type :
- Academic Journal
- Accession number :
- 22753847
- Full Text :
- https://doi.org/10.1128/EC.00075-12