© The Rockefeller University Press,
0021-9525/1998//1347 $5.00
The Journal of Cell Biology, Volume 140, Number 6,
, 1998 1347-1356
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
Meng-Chieh Chiang and
Hui-Ling Chiang
Department of Cell Biology, Harvard Medical School, Boston, Massachussets 02115
Glucose regulates the degradation of the key gluconeogenic enzyme, fructose-1,6-bisphosphatase (FBPase), in Saccharomyces cerevisiae. FBPase is targeted from the cytosol to a novel type of vesicle, and then to the vacuole for degradation when yeast cells are transferred from medium containing poor carbon sources to fresh glucose. To identify proteins involved in the FBPase degradation pathway, we cloned our first VID (vacuolar import and degradation) gene. The VID24 gene was identified by complementation of the FBPase degradation defect of the vid24-1 mutant. Vid24p is a novel protein of 41 kD and is synthesized in response to glucose. Vid24p is localized to the FBPase-containing vesicles as a peripheral membrane protein. In the absence of functional Vid24p, FBPase accumulates in the vesicles and fails to move to the vacuole, suggesting that Vid24p regulates FBPase targeting from the vesicles to the vacuole. FBPase sequestration into the vesicles is not affected in the vid24-1 mutant, indicating that Vid24p acts after FBPase sequestration into the vesicles has occurred. Vid24p is the first protein identified that marks the FBPase-containing vesicles and plays a critical role in delivering FBPase from the vesicles to the vacuole for degradation.
Abbreviations used in this paper: COP, coat protein; CPY, carboxypeptidase Y; ECL, enhanced chemiluminescence; FBPase, fructose-1,6-bisphosphatase; G-6-P, glucose-6-phosphate; HA, hemagglutinin; VID, vacuolar import and degradation.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Facebook 
Reddit 
Technorati 
Twitter What's this?
This article has been cited by other articles:
-
Brown, C. R., Wolfe, A. B., Cui, D., Chiang, H.-L.
(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: 26116-26127
[Abstract]
[Full Text]
-
Santt, O., Pfirrmann, T., Braun, B., Juretschke, J., Kimmig, P., Scheel, H., Hofmann, K., Thumm, M., Wolf, D. H.
(2008). The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism. Mol. Biol. Cell
19: 3323-3333
[Abstract]
[Full Text]
-
Soontorngun, N., Larochelle, M., Drouin, S., Robert, F., Turcotte, B.
(2007). Regulation of Gluconeogenesis in Saccharomyces cerevisiae Is Mediated by Activator and Repressor Functions of Rds2. Mol. Cell. Biol.
27: 7895-7905
[Abstract]
[Full Text]
-
Slattery, M. G., Liko, D., Heideman, W.
(2006). The Function and Properties of the Azf1 Transcriptional Regulator Change with Growth Conditions in Saccharomyces cerevisiae. Eukaryot Cell
5: 313-320
[Abstract]
[Full Text]
-
Hung, G.-C., Brown, C. R., Wolfe, A. B., Liu, J., Chiang, H.-L.
(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: 49138-49150
[Abstract]
[Full Text]
-
Cui, D.-Y., Brown, C. R., Chiang, H.-L.
(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: 9713-9724
[Abstract]
[Full Text]
-
Kaniak, A., Xue, Z., Macool, D., Kim, J.-H., Johnston, M.
(2004). Regulatory Network Connecting Two Glucose Signal Transduction Pathways in Saccharomyces cerevisiae. Eukaryot Cell
3: 221-231
[Abstract]
[Full Text]
-
Brown, C. R., Liu, J., Hung, G.-C., Carter, D., Cui, D., Chiang, H.-L.
(2003). The Vid Vesicle to Vacuole Trafficking Event Requires Components of the SNARE Membrane Fusion Machinery. J. Biol. Chem.
278: 25688-25699
[Abstract]
[Full Text]
-
Regelmann, J., Schule, T., Josupeit, F. S., Horak, J., Rose, M., Entian, K.-D., Thumm, M., Wolf, D. H.
(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: 1652-1663
[Abstract]
[Full Text]
-
Brown, C. R., McCann, J. A., Hung, G. G.-C., Elco, C. P., Chiang, H.-L.
(2002). Vid22p, a novel plasma membrane protein, is required for the fructose-1,6-bisphosphatase degradation pathway. J. Cell Sci.
115: 655-666
[Abstract]
[Full Text]
-
Brown, C. R., Cui, D.-Y., Hung, G. G.-C., Chiang, H.-L.
(2001). Cyclophilin A Mediates Vid22p Function in the Import of Fructose-1,6-bisphosphatase into Vid Vesicles. J. Biol. Chem.
276: 48017-48026
[Abstract]
[Full Text]
-
Brown, C. R., McCann, J. A., Chiang, H.-L.
(2000). The Heat Shock Protein Ssa2p Is Required for Import of Fructose-1,6-Bisphosphatase into Vid Vesicles. JCB
150: 65-76
[Abstract]
[Full Text]
-
Horst, M., Knecht, E. C., Schu, P. V.
(1999). Import into and Degradation of Cytosolic Proteins by Isolated Yeast Vacuoles. Mol. Biol. Cell
10: 2879-2889
[Abstract]
[Full Text]
-
Salvador, N., Aguado, C., Horst, M., Knecht, E.
(2000). Import of a Cytosolic Protein into Lysosomes by Chaperone-mediated Autophagy Depends on Its Folding State. J. Biol. Chem.
275: 27447-27456
[Abstract]
[Full Text]
-
Shieh, H.-L., Chen, Y., Brown, C. R., Chiang, H.-L.
(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: 10398-10406
[Abstract]
[Full Text]
