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Literature summary for 3.1.3.11 extracted from

  • Giardina, B.J.; Chiang, H.L.
    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 (2013), Plant Signal. Behav., 8, e24936.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm fructose-1,6-bisphosphatase is secreted into the periplasm during prolonged glucose starvation and is internalized into vacuole import and degradation vesicles/endosomes following glucose re-feeding. Fructose-1,6-bisphosphatase does not contain signal sequences required for the classical secretory and endocytic pathways, the secretion and internalization are mediated via the non-classical pathways and involves protein Vps34, which is involved in multiple protein trafficking events Saccharomyces cerevisiae
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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General Information

General Information Comment Organism
metabolism fructose-1,6-bisphosphatase is secreted into the periplasm during prolonged glucose starvation and is internalized into vacuole import and degradation vesicles/endosomes following glucose re-feeding. Fructose-1,6-bisphosphatase does not contain signal sequences required for the classical secretory and endocytic pathways, the secretion and internalization are mediated via the non-classical pathways and involves protein Vps34, which is involved in multiple protein trafficking events Saccharomyces cerevisiae