Exocytosis and endocytosis of small vesicles across the plasma membrane in Saccharomyces cerevisiae

Kathryn Stein, Hui-ling Chiang

Research output: Contribution to journalReview article

4 Citations (Scopus)

Abstract

When Saccharomyces cerevisiae is starved of glucose, the gluconeogenic enzymes fructose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase, isocitrate lyase, and malate dehydrogenase, as well as the non-gluconeogenic enzymes glyceraldehyde-3-phosphate dehydrogenase and cyclophilin A, are secreted into the periplasm. In the extracellular fraction, these secreted proteins are associated with small vesicles that account for more than 90% of the total number of extracellular structures observed. When glucose is added to glucose-starved cells, FBPase is internalized and associated with clusters of small vesicles in the cytoplasm. Specifically, the internalization of FBPase results in the decline of FBPase and vesicles in the extracellular fraction and their appearance in the cytoplasm. The clearance of extracellular vesicles and vesicle-associated proteins from the extracellular fraction is dependent on the endocytosis gene END3. This internalization is regulated when cells are transferred from low to high glucose. It is rapidly occurring and is a high capacity process, as clusters of vesicles occupy 10%–20% of the total volume in the cytoplasm in glucose re-fed cells. FBPase internalization also requires the VPS34 gene encoding PI3K. Following internalization, FBPase is delivered to the vacuole for degradation, whereas proteins that are not degraded may be recycled.

Original languageEnglish (US)
Pages (from-to)608-629
Number of pages22
JournalMembranes
Volume4
Issue number3
DOIs
StatePublished - Sep 3 2014

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Fructose-Bisphosphatase
Fructose
Cell membranes
Yeast
Glucose
Proteins
Enzymes
Isocitrate Lyase
Cyclophilin A
Malate Dehydrogenase
Phosphoenolpyruvate
Glyceraldehyde-3-Phosphate Dehydrogenases
Gene encoding
Phosphatidylinositol 3-Kinases
Phosphates
Genes
Degradation

All Science Journal Classification (ASJC) codes

  • Materials Science(all)

Cite this

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title = "Exocytosis and endocytosis of small vesicles across the plasma membrane in Saccharomyces cerevisiae",
abstract = "When Saccharomyces cerevisiae is starved of glucose, the gluconeogenic enzymes fructose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase, isocitrate lyase, and malate dehydrogenase, as well as the non-gluconeogenic enzymes glyceraldehyde-3-phosphate dehydrogenase and cyclophilin A, are secreted into the periplasm. In the extracellular fraction, these secreted proteins are associated with small vesicles that account for more than 90{\%} of the total number of extracellular structures observed. When glucose is added to glucose-starved cells, FBPase is internalized and associated with clusters of small vesicles in the cytoplasm. Specifically, the internalization of FBPase results in the decline of FBPase and vesicles in the extracellular fraction and their appearance in the cytoplasm. The clearance of extracellular vesicles and vesicle-associated proteins from the extracellular fraction is dependent on the endocytosis gene END3. This internalization is regulated when cells are transferred from low to high glucose. It is rapidly occurring and is a high capacity process, as clusters of vesicles occupy 10{\%}–20{\%} of the total volume in the cytoplasm in glucose re-fed cells. FBPase internalization also requires the VPS34 gene encoding PI3K. Following internalization, FBPase is delivered to the vacuole for degradation, whereas proteins that are not degraded may be recycled.",
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Exocytosis and endocytosis of small vesicles across the plasma membrane in Saccharomyces cerevisiae. / Stein, Kathryn; Chiang, Hui-ling.

In: Membranes, Vol. 4, No. 3, 03.09.2014, p. 608-629.

Research output: Contribution to journalReview article

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