FBP1/YLR377C Literature Guide Help

Other names published for FBP1: ACN8, fructose 1,6-bisphosphate 1-phosphatase, YLR377C

FBP1 - Protein Processing/Modification/Regulation (44)

Results: 1 - 30 of 44 records
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ReferenceOther Genes Addressed
Cao S, et al.  (2012) A Mitochondria-Dependent Pathway Mediates the Apoptosis of GSE-Induced Yeast. PLoS One 7(3):e32943
Giardina BJ, et al.  (2012) Comparative Proteomic Analysis of Transition of Saccharomyces cerevisiae from Glucose-Deficient Medium to Glucose-Rich Medium. Proteome Sci 10(1):40
Oliveira AP, et al.  (2012) Regulation of yeast central metabolism by enzyme phosphorylation. Mol Syst Biol 8():623
Barbin L, et al.  (2010) The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase. Biochem Biophys Res Commun 394(2):335-41
Brown CR, et al.  (2010) The TOR complex 1 is distributed in endosomes and in retrograde vesicles that form from the vacuole membrane and plays an important role in the vacuole import and degradation pathway. J Biol Chem 285(30):23359-70
Brown CR, et al.  (2010) The vacuole import and degradation pathway utilizes early steps of endocytosis and actin polymerization to deliver cargo proteins to the vacuole for degradation. J Biol Chem 285(2):1516-28
Yan Y and Kang B  (2010) Regulation of Vid-dependent degradation of FBPase by TCO89, a component of TOR Complex 1. Int J Biol Sci 6(4):361-70
Brown CR, et al.  (2008) The vacuolar import and degradation pathway merges with the endocytic pathway to deliver fructose-1,6-bisphosphatase to the vacuole for degradation. J Biol Chem 283(38):26116-27
Santt O, et al.  (2008) The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism. Mol Biol Cell 19(8):3323-33
Belinchon MM and Gancedo JM  (2007) Glucose controls multiple processes in Saccharomyces cerevisiae through diverse combinations of signaling pathways. FEMS Yeast Res 7(6):808-18
Liu J, et al.  (2005) Degradation of the gluconeogenic enzyme fructose-1, 6-bisphosphatase is dependent on the vacuolar ATPase. Autophagy 1(3):146-56
Cui DY, et al.  (2004) The type 1 phosphatase Reg1p-Glc7p is required for the glucose-induced degradation of fructose-1,6-bisphosphatase in the vacuole. J Biol Chem 279(11):9713-24
Hung GC, et al.  (2004) Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events. J Biol Chem 279(47):49138-50
Brown CR, et al.  (2003) The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery. J Biol Chem 278(28):25688-99
Regelmann J, et al.  (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63
Brown CR, et al.  (2002) Vid22p, a novel plasma membrane protein, is required for the fructose-1,6-bisphosphatase degradation pathway. J Cell Sci 115(Pt 3):655-66
Horak J, et al.  (2002) Two distinct proteolytic systems responsible for glucose-induced degradation of fructose-1,6-bisphosphatase and the Gal2p transporter in the yeast Saccharomyces cerevisiae share the same protein components of the glucose signaling pathway. J Biol Chem 277(10):8248-54
Monribot-Espagne C and Boucherie H  (2002) Differential gel exposure, a new methodology for the two-dimensional comparison of protein samples. Proteomics 2(3):229-40
Brown CR, et al.  (2001) Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles. J Biol Chem 276(51):48017-26
Shieh HL, et al.  (2001) Biochemical analysis of fructose-1,6-bisphosphatase import into vacuole import and degradation vesicles reveals a role for UBC1 in vesicle biogenesis. J Biol Chem 276(13):10398-406
Brown CR, et al.  (2000) The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles. J Cell Biol 150(1):65-76
Schule T, et al.  (2000) Ubc8p functions in catabolite degradation of fructose-1, 6-bisphosphatase in yeast. EMBO J 19(10):2161-7
Chiang MC and Chiang HL  (1998) Vid24p, a novel protein localized to the fructose-1, 6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation. J Cell Biol 140(6):1347-56
Hammerle M, et al.  (1998) Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. J Biol Chem 273(39):25000-5
Shieh HL and Chiang HL  (1998) In vitro reconstitution of glucose-induced targeting of fructose-1, 6-bisphosphatase into the vacuole in semi-intact yeast cells. J Biol Chem 273(6):3381-7
Huang PH and Chiang HL  (1997) Identification of novel vesicles in the cytosol to vacuole protein degradation pathway. J Cell Biol 136(4):803-10
Chiang HL, et al.  (1996) Selective uptake of cytosolic, peroxisomal, and plasma membrane proteins into the yeast lysosome for degradation. J Biol Chem 271(17):9934-41
Hoffman M and Chiang HL  (1996) Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae. Genetics 143(4):1555-66
Schork SM, et al.  (1995) Catabolite inactivation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. Degradation occurs via the ubiquitin pathway. J Biol Chem 270(44):26446-50
de Jong-Gubbels P, et al.  (1995) Regulation of carbon metabolism in chemostat cultures of Saccharomyces cerevisiae grown on mixtures of glucose and ethanol. Yeast 11(5):407-18
Results: 1 - 30 of 44 records
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