title: 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.
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.
authors.affiliation: Department of Cellular and Molecular Physiology; Penn State College of Medicine; Hershey, PA USA.
authors.forename: Bennett J
authors.initials: BJ
authors.lastname: Giardina
authors.forename: Hui-Ling
authors.initials: HL
authors.lastname: Chiang
mesh_terms: D004705:Endocytosis; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D005943:Gluconeogenesis; D005947:Glucose / Q000172:deficiency*; D012441:Saccharomyces cerevisiae / Q000166:cytology* / Q000201:enzymology*; D055571:Secretory Pathway
chemical_list: D006597:Fructose-Bisphosphatase; D005947:Glucose
keywords: PI3K; fructose-1,6-bisphosphatase; gluconeogenesis; non-classical secretion and endocytosis; vacuole import and degradation