High impact information on VID30

• Several vid mutants defective in the glucose-induced degradation of FBPase in the vacuole have been isolated [1].
• Ammonia regulates VID30 expression and Vid30p function shifts nitrogen metabolism toward glutamate formation especially when Saccharomyces cerevisiae is grown in low concentrations of ammonia [2].
• Patterns of gene expression in a vid30 Delta suggest that the Vid30p function shifts the balance of nitrogen metabolism toward the production of glutamate, especially when cells are grown in low ammonia [2].
• Glucose-induced degradation of the MDH2 isozyme of malate dehydrogenase in yeast [3].
• We used mutation analysis to identify target sequences in Mal61/HA maltose permease involved in its selective glucose-induced degradation [4].

Biological context of VID30

• Glucose-induced degradation of yeast fructose-1,6-bisphosphatase requires additional triggering events besides protein phosphorylation [5].
• GID1 overexpression resulted in a GA-hypersensitive phenotype [6].

Associations of VID30 with chemical compounds

• The decreased rate of glucose-induced degradation correlates with a decrease in the level of glucose-induced ubiquitination of the DeltaPEST mutant permease [4].
• Results indicate that the proline-, glutamate-, aspartate-, serine-, and threonine-rich (PEST) sequence found in the N-terminal cytoplasmic domain, particularly residues 49-78, is required for glucose-induced degradation of Mal61/HAp and for the rapid glucose-induced inactivation of maltose transport activity [4].

Enzymatic interactions of VID30

• In this report, we show that MDH2 is phosphorylated during the process of glucose-induced degradation [7].

Other interactions of VID30

• We also show that Reg1 and yeast 14-3-3 proteins participate actively in the regulation of the glucose-induced degradation of maltose permease (Mal61) [8].
• This glucose-induced degradation is independent of the proteasome but requires ubiquitin and certain ubiquitin conjugating enzymes [4].

References