JBC Biosymposia, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on March 12, 2004
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
279/11/9713    most recent
M310793200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cui, D.-Y.
Right arrow Articles by Chiang, H.-L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cui, D.-Y.
Right arrow Articles by Chiang, H.-L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print December 18, 2003
J. Biol. Chem, 10.1074/jbc.M310793200
Submitted on October 1, 2003
Revised on November 28, 2003
Accepted on December 18, 2003

The type 1 phosphatase reg1p/Glc7p is required for the glucose-induced degradation of fructose-1,6-bisphosphatase in the vacuole

Dong-Ying Cui, C. Randell Brown, and Hui-Ling Chiang

Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, PA 17033

Corresponding Author: crb13{at}psu.edu

Protein phosphatases play an important role in vesicular trafficking and membrane fusion processes. The type 1 phosphatase Glc7p and its regulatory subunit Reg1p were identified as required components in the glucose-induced targeting of the key gluconeogenic enzyme fructose-1, 6-bisphosphatase (FBPase) to the vacuole for degradation. The interaction of Reg1p with Glc7p was important for the transport of FBPase from intermediate Vid vesicles to vacuoles. The glc7-T152K mutant strain exhibited a reduced Reg1p binding, along with defects in FBPase degradation and Vid vesicle trafficking to the vacuole. In this mutant, Vid vesicles were the most defective components, whereas the vacuole was also defective. Shp1p and Glc8p regulate Glc7p phosphatase activity and are required for FBPase degradation. In the delta shp1 and delta glc8 strains, Reg1p-Glc7p interaction was not affected, suggesting that phosphatase activity is also necessary for FBPase degradation. Similar to those seen in the glc7-T152K mutant, the delta shp1 and delta glc8 mutants exhibited severely defective Vid vesicles, but partially defective vacuoles. Taken together, our results suggest that Reg1p/Glc7p interaction and Glc7p phosphatase activity play a required role in the Vid vesicle to vacuole trafficking step along the FBPase degradation pathway.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Microbiol. Mol. Biol. Rev.Home page
G. M. Santangelo
Glucose Signaling in Saccharomyces cerevisiae
Microbiol. Mol. Biol. Rev., March 1, 2006; 70(1): 253 - 282.
[Abstract] [Full Text] [PDF]

Home page
 GeneticsHome page
H. Cai, S. Kauffman, F. Naider, and J. M. Becker
Genomewide Screen Reveals a Wide Regulatory Network for Di/Tripeptide Utilization in Saccharomyces cerevisiae
Genetics, March 1, 2006; 172(3): 1459 - 1476.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G.-C. Hung, C. R. Brown, A. B. Wolfe, J. Liu, and H.-L. Chiang
Degradation of the Gluconeogenic Enzymes Fructose-1,6-bisphosphatase and Malate Dehydrogenase Is Mediated by Distinct Proteolytic Pathways and Signaling Events
J. Biol. Chem., November 19, 2004; 279(47): 49138 - 49150.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.