Vid22p, a novel plasma membrane protein, is required for the fructose-1, 6-bisphosphatase degradation pathway

C. Randell Brown, Jameson A. McCann, Graham Guo Chiuan Hung, Christopher P. Elco, Hui Ling Chiang

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Fructose-1,6-bisphosphatase (FBPase), an important enzyme in the gluconeogenic pathway in Saccharomyces cerevisiae, is expressed when cells are grown in media containing a poor carbon source. Following glucose replenishment, FBPase is targeted from the cytosol to intermediate Vid (vacuole import and degradation) vesicles and then to the vacuole for degradation. Recently, several vid mutants that are unable to degrade FBPase in response to glucose were identified. Here, we present VID22, a novel gene involved in FBPase degradation. VID22 encodes a glycosylated integral membrane protein that localizes to the plasma membrane. Newly synthesized Vid22p was found in the cytoplasm and then targeted to the plasma membrane independent of the classical secretory pathway. A null mutation of VID22 failed to degrade FBPase following a glucose shift and accumulated FBPase in the cytosol. Furthermore, the majority of FBPase remained in a proteinase K sensitive compartment in the Δvid22 mutant, implying that VID22 is involved in FBPase transport from the cytosol to Vid vesicles. By contrast, starvation-induced autophagy and peroxisome degradation were not impaired in the Δvid22 mutant. This strain also exhibited the proper processing of carboxypeptidase Y and aminopeptidase I in the vacuole. Therefore, Vid22p appears to play a specific role in the FBPase trafficking pathway.

Original languageEnglish (US)
Pages (from-to)655-666
Number of pages12
JournalJournal of Cell Science
Volume115
Issue number3
StatePublished - Feb 1 2002

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Fructose-Bisphosphatase
Blood Proteins
Membrane Proteins
Cell Membrane
Vacuoles
Cytosol
Glucose
Cathepsin A
Endopeptidase K
Aminopeptidases
Peroxisomes
Secretory Pathway
Autophagy
Starvation
Saccharomyces cerevisiae
Cytoplasm
Carbon

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

Randell Brown, C. ; McCann, Jameson A. ; Hung, Graham Guo Chiuan ; Elco, Christopher P. ; Chiang, Hui Ling. / Vid22p, a novel plasma membrane protein, is required for the fructose-1, 6-bisphosphatase degradation pathway. In: Journal of Cell Science. 2002 ; Vol. 115, No. 3. pp. 655-666.
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abstract = "Fructose-1,6-bisphosphatase (FBPase), an important enzyme in the gluconeogenic pathway in Saccharomyces cerevisiae, is expressed when cells are grown in media containing a poor carbon source. Following glucose replenishment, FBPase is targeted from the cytosol to intermediate Vid (vacuole import and degradation) vesicles and then to the vacuole for degradation. Recently, several vid mutants that are unable to degrade FBPase in response to glucose were identified. Here, we present VID22, a novel gene involved in FBPase degradation. VID22 encodes a glycosylated integral membrane protein that localizes to the plasma membrane. Newly synthesized Vid22p was found in the cytoplasm and then targeted to the plasma membrane independent of the classical secretory pathway. A null mutation of VID22 failed to degrade FBPase following a glucose shift and accumulated FBPase in the cytosol. Furthermore, the majority of FBPase remained in a proteinase K sensitive compartment in the Δvid22 mutant, implying that VID22 is involved in FBPase transport from the cytosol to Vid vesicles. By contrast, starvation-induced autophagy and peroxisome degradation were not impaired in the Δvid22 mutant. This strain also exhibited the proper processing of carboxypeptidase Y and aminopeptidase I in the vacuole. Therefore, Vid22p appears to play a specific role in the FBPase trafficking pathway.",
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Vid22p, a novel plasma membrane protein, is required for the fructose-1, 6-bisphosphatase degradation pathway. / Randell Brown, C.; McCann, Jameson A.; Hung, Graham Guo Chiuan; Elco, Christopher P.; Chiang, Hui Ling.

In: Journal of Cell Science, Vol. 115, No. 3, 01.02.2002, p. 655-666.

Research output: Contribution to journalArticle

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