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Review
. 2013 Aug;8(8):e24936.
doi: 10.4161/psb.24936. Epub 2013 Jun 26.

The key gluconeogenic enzyme fructose-1,6-bisphosphatase is secreted during prolonged glucose starvation and is internalized following glucose re-feeding via the non-classical secretory and internalizing pathways in Saccharomyces cerevisiae

Bennett J Giardina  1 , Hui-Ling Chiang
Affiliations
Review

The key gluconeogenic enzyme fructose-1,6-bisphosphatase is secreted during prolonged glucose starvation and is internalized following glucose re-feeding via the non-classical secretory and internalizing pathways in Saccharomyces cerevisiae

Bennett J Giardina et al. Plant Signal Behav. 2013 Aug.

Abstract

In Saccharomyces cerevisia, the key gluconeogenic enzyme fructose-1,6-bisphosphatase is secreted into the periplasm during prolonged glucose starvation and is internalized into Vid/endosomes following glucose re-feeding. Fructose-1,6-bisphosphatase does not contain signal sequences required for the classical secretory and endocytic pathways. Hence, the secretion and internalization are mediated via the non-classical pathways.

Keywords: PI3K; fructose-1,6-bisphosphatase; gluconeogenesis; non-classical secretion and endocytosis; vacuole import and degradation.

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Figures

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Figure 1. A model for the Vid pathway. When wild-type cells are starved of glucose for a prolonged period of time, significant amounts of FBPase are secreted into the periplasm. Following glucose re-feeding, FBPase is internalized into Vid/endosomes. The internalization of FBPase requires the SLA1, ARC18 and VPS34 genes. Under the same conditions, most of the Vid24p, Sec28p, Vid30p and Vps34p are in the intracellular fraction. Vid24p, Sec28p and Vid30p associate with actin patches initially and dissociate later, whereas Vps34p associates with actin patches constitutively. Following internalization, FBPase is targeted to the vacuole and then degraded in the lumen.
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