A selective autophagy pathway that degrades gluconeogenic enzymes during catabolite inactivation

C. Randell Brown, Hui-ling Chiang

Research output: Contribution to journalShort survey

15 Scopus citations

Abstract

In Saccharomyces cerevisiae, glucose starvation induces key gluconeogenic enzymes such as fructose-1,6-bisphosphatase (FBPase), malate dehydrogenase (MDH2) and phosphoenolpyruvate carboxykinase, while glucose addition inactivates these enzymes. Significant progress has been made identifying mechanisms that mediate the "catabolite inactivation" of FBPase and MDH2. For example, the site of their degradation has been shown to change, depending on the duration of starvation. When glucose is added to short-termed starved cells, these proteins are degraded in the proteasome. However, when glucose is added to long-termed starved cells, they are degraded in the vacuole by a selective autophagy pathway. For the vacuole pathway, these proteins are first imported into novel vesicles called Vid (vacuole import and degradation) vesicles. Following import, Vid vesicles merge with the endocytic pathway. Future experiments will be directed at understanding the molecular mechanisms that regulate the switch from proteasomal to vacuolar degradation and determining the site of Vid vesicle biogenesis.

Original languageEnglish (US)
Pages (from-to)177-183
Number of pages7
JournalCommunicative and Integrative Biology
Volume2
Issue number2
StatePublished - Mar 1 2009

All Science Journal Classification (ASJC) codes

  • Agricultural and Biological Sciences(all)

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