The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery

C. Randell Brown, Jingjing Liu, Guo Chiuan Hung, Donald Carter, Dongying Cui, Hui-ling Chiang

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is targeted to Vid vesicles when glucose-starved cells are replenished with glucose. Vid vesicles then deliver FBPase to the vacuole for degradation. A modified alkaline phosphatase assay was developed to study the trafficking of Vid vesicles to the vacuole. For this assay, FBPase was fused with a truncated form of alkaline phosphatase. Under in vivo conditions, FBPase-Δ60Pho8p was targeted to the vacuole via Vid vesicles, and it exhibited Pep4p- and Vid24p-dependent alkaline phosphatase activation. Vid vesicle-vacuole targeting was reconstituted using Vid vesicles that contained FBPase-Δ60Pho8p. These vesicles were incubated with vacuoles in the presence of cytosol and an ATP-regenerating system. Under in vitro conditions, alkaline phosphatase was also activated in a Pep4p- and Vid24p-dependent manner. The GTPase Ypt7p was identified as an essential component in Vid vesicle-vacuole trafficking. Likewise, a number of v-SNAREs (Ykt6p, Nyv1p, Vti1p) and homotypic fusion vacuole protein sorting complex family members (Vps39p and Vps41p) were required for the proper function of Vid vesicles. In contrast, the T-SNARE Vam3p was a necessary vacuolar component. Vid vesicle-vacuole trafficking exhibits characteristics similar to heterotypic membrane fusion events.

Original languageEnglish (US)
Pages (from-to)25688-25699
Number of pages12
JournalJournal of Biological Chemistry
Volume278
Issue number28
DOIs
StatePublished - Jul 11 2003

Fingerprint

Fructose-Bisphosphatase
SNARE Proteins
Membrane Fusion
Vacuoles
Machinery
Fusion reactions
Alkaline Phosphatase
Membranes
Assays
Glucose
GTP Phosphohydrolases
Sorting
Adenosine Triphosphate
Chemical activation
Protein Transport
Degradation
Cytosol
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Brown, C. Randell ; Liu, Jingjing ; Hung, Guo Chiuan ; Carter, Donald ; Cui, Dongying ; Chiang, Hui-ling. / The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery. In: Journal of Biological Chemistry. 2003 ; Vol. 278, No. 28. pp. 25688-25699.
@article{2edc25aed93a4275b27a2614869c92a1,
title = "The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery",
abstract = "The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is targeted to Vid vesicles when glucose-starved cells are replenished with glucose. Vid vesicles then deliver FBPase to the vacuole for degradation. A modified alkaline phosphatase assay was developed to study the trafficking of Vid vesicles to the vacuole. For this assay, FBPase was fused with a truncated form of alkaline phosphatase. Under in vivo conditions, FBPase-Δ60Pho8p was targeted to the vacuole via Vid vesicles, and it exhibited Pep4p- and Vid24p-dependent alkaline phosphatase activation. Vid vesicle-vacuole targeting was reconstituted using Vid vesicles that contained FBPase-Δ60Pho8p. These vesicles were incubated with vacuoles in the presence of cytosol and an ATP-regenerating system. Under in vitro conditions, alkaline phosphatase was also activated in a Pep4p- and Vid24p-dependent manner. The GTPase Ypt7p was identified as an essential component in Vid vesicle-vacuole trafficking. Likewise, a number of v-SNAREs (Ykt6p, Nyv1p, Vti1p) and homotypic fusion vacuole protein sorting complex family members (Vps39p and Vps41p) were required for the proper function of Vid vesicles. In contrast, the T-SNARE Vam3p was a necessary vacuolar component. Vid vesicle-vacuole trafficking exhibits characteristics similar to heterotypic membrane fusion events.",
author = "Brown, {C. Randell} and Jingjing Liu and Hung, {Guo Chiuan} and Donald Carter and Dongying Cui and Hui-ling Chiang",
year = "2003",
month = "7",
day = "11",
doi = "10.1074/jbc.M210549200",
language = "English (US)",
volume = "278",
pages = "25688--25699",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "28",

}

The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery. / Brown, C. Randell; Liu, Jingjing; Hung, Guo Chiuan; Carter, Donald; Cui, Dongying; Chiang, Hui-ling.

In: Journal of Biological Chemistry, Vol. 278, No. 28, 11.07.2003, p. 25688-25699.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery

AU - Brown, C. Randell

AU - Liu, Jingjing

AU - Hung, Guo Chiuan

AU - Carter, Donald

AU - Cui, Dongying

AU - Chiang, Hui-ling

PY - 2003/7/11

Y1 - 2003/7/11

N2 - The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is targeted to Vid vesicles when glucose-starved cells are replenished with glucose. Vid vesicles then deliver FBPase to the vacuole for degradation. A modified alkaline phosphatase assay was developed to study the trafficking of Vid vesicles to the vacuole. For this assay, FBPase was fused with a truncated form of alkaline phosphatase. Under in vivo conditions, FBPase-Δ60Pho8p was targeted to the vacuole via Vid vesicles, and it exhibited Pep4p- and Vid24p-dependent alkaline phosphatase activation. Vid vesicle-vacuole targeting was reconstituted using Vid vesicles that contained FBPase-Δ60Pho8p. These vesicles were incubated with vacuoles in the presence of cytosol and an ATP-regenerating system. Under in vitro conditions, alkaline phosphatase was also activated in a Pep4p- and Vid24p-dependent manner. The GTPase Ypt7p was identified as an essential component in Vid vesicle-vacuole trafficking. Likewise, a number of v-SNAREs (Ykt6p, Nyv1p, Vti1p) and homotypic fusion vacuole protein sorting complex family members (Vps39p and Vps41p) were required for the proper function of Vid vesicles. In contrast, the T-SNARE Vam3p was a necessary vacuolar component. Vid vesicle-vacuole trafficking exhibits characteristics similar to heterotypic membrane fusion events.

AB - The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is targeted to Vid vesicles when glucose-starved cells are replenished with glucose. Vid vesicles then deliver FBPase to the vacuole for degradation. A modified alkaline phosphatase assay was developed to study the trafficking of Vid vesicles to the vacuole. For this assay, FBPase was fused with a truncated form of alkaline phosphatase. Under in vivo conditions, FBPase-Δ60Pho8p was targeted to the vacuole via Vid vesicles, and it exhibited Pep4p- and Vid24p-dependent alkaline phosphatase activation. Vid vesicle-vacuole targeting was reconstituted using Vid vesicles that contained FBPase-Δ60Pho8p. These vesicles were incubated with vacuoles in the presence of cytosol and an ATP-regenerating system. Under in vitro conditions, alkaline phosphatase was also activated in a Pep4p- and Vid24p-dependent manner. The GTPase Ypt7p was identified as an essential component in Vid vesicle-vacuole trafficking. Likewise, a number of v-SNAREs (Ykt6p, Nyv1p, Vti1p) and homotypic fusion vacuole protein sorting complex family members (Vps39p and Vps41p) were required for the proper function of Vid vesicles. In contrast, the T-SNARE Vam3p was a necessary vacuolar component. Vid vesicle-vacuole trafficking exhibits characteristics similar to heterotypic membrane fusion events.

UR - http://www.scopus.com/inward/record.url?scp=0037815080&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037815080&partnerID=8YFLogxK

U2 - 10.1074/jbc.M210549200

DO - 10.1074/jbc.M210549200

M3 - Article

VL - 278

SP - 25688

EP - 25699

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 28

ER -